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  • 1.
    Baradaran-Heravi, A.
    et al.
    Division of Human Genetics, Immunology Research Centre, Bu-Ali Research Institute, Mashhad, Iran.
    Vakili, R.
    Department of Paediatrics, Imam Reza Hospital, Mashhad University of Medical Sciences (MUMS), Mashhad, Iran.
    Robins, T.
    Department of Molecular Medicine and Surgery, Centre of Molecular Medicine (CMM) L8:02, Karolinska Institutet/Karolinska University Hospital, Stockholm, Sweden.
    Carlsson, Jenny
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Applied Physics .
    Ghaemi, N.
    Department of Paediatrics, Imam Reza Hospital, Mashhad University of Medical Sciences (MUMS), Mashhad, Iran.
    A'Rabi, A.
    Division of Human Genetics, Immunology Research Centre, Bu-Ali Research Institute, Mashhad, Iran.
    Abbaszadegan, M.R.
    Division of Human Genetics, Bu-Ali Research Institute, Mashhad University of Medical Sciences, PO Box 9196773117, Mashhad, Iran, Division of Human Genetics, Immunology Research Centre, Bu-Ali Research Institute, Mashhad, Iran.
    Three novel CYP21A2 mutations and their protein modelling in patients with classical 21-hydroxylase deficiency from northeastern Iran2007In: Clinical Endocrinology, ISSN 0300-0664, E-ISSN 1365-2265, Vol. 67, no 3, p. 335-341Article in journal (Refereed)
    Abstract [en]

    Objective: Congenital adrenal hyperplasia (CAH) refers to a group of autosomal recessive disorders frequently caused by mutations in the steroid 21-hydroxylase gene (CYP21A2). We describe three novel CYP21A2 mutations in CAH patients. Design and methods: Sequence analysis of the entire CYP21A2 gene followed by molecular modelling was performed in three unrelated classical CAH patients of northeastern Iranian origin. The active (CYP21A2) and pseudogene (CYP21A1P) alleles were screened for the presence of the new variations in controls. Results: Two novel missense mutations, F404S in exon 9 and T450P in exon 10, were found in homozygous forms in two female patients with a salt-wasting (SW) phenotype. These novel variants were screened by allele-specific polymerase chain reaction (PCR) and excluded in 100 unrelated normal alleles. Prediction of clinical severity, based on molecular modelling and sequence conservation, correlates well with the clinical diagnosis of the patients carrying these mutations. The third novel mutation, a small 10-bp deletion in exon 1, g.19_28del, was found in a female patient with a simple virilizing phenotype in a compound heterozygous form with the common intron 2 splice mutation (IVS2-13A/C>G). This frameshift mutation causes a premature stop codon at amino acid position 48, L48X, resulting in a nonfunctional protein. The CYP21A1P pseudogene alleles were also screened and none of these novel mutations could be detected. Conclusions: Three novel mutations were found in the CYP21A2 gene and predicted to drastically impair enzyme activity resulting in severe classic CAH. None of these mutations occurs in the CYP21A1P pseudogene. © 2007 The Authors.

  • 2.
    Carlsson, Jenny
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics . Linköping University, The Institute of Technology.
    Interaction Studies in Complex Fluids with Optical Biosensors2008Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    In this thesis interactions in complex fluids, such as serum and meat juice, were analysed with optical biosensor techniques.

    Panels of lectins immobilised on gold surfaces were used for investigation of differences in protein glycosylation pattern in sera and meat juices between various species. The present panel was also used for investigation of global glycosylation changes of serum proteins in type 1 diabetes patients. Biorecognition was evaluated with null ellipsometry and scanning ellipsometry combined with multivariate data analysis techniques (MVDA). Principal component analysis (PCA) showed that the lectin panel enabled discrimination between sera from the different species as well as for the different meat juices. The results also indicate that there is a measurable global alteration in glycosylation pattern of serum proteins in type 1 diabetic patients compared to healthy subjects. Using an artificial neuronal net (ANN), it was also possible to correctly categorise unknown serum samples into their respective class or group. The analytical potential of combining information from lectin panels with multivariate data analysis was thereby demonstrated.

    Also, a sensitive and specific method based on surface plasmon resonance (SPR) for detection of insulin autoantibodies (IAA) in serum samples from individuals at high risk of developing type 1 diabetes (T1D) has been developed. When measuring trace molecules, such as autoantibodies, in undiluted sera with label-free techniques like SPR, non-specific adsorption of matrix proteins to the sensor surface is often a problem, since it causes a signal that masks the analyte response. The developed method is an indirect competitive immunoassay designed to overcome these problems. Today, IAA is mainly measured in radio immunoassays (RIAs), which are time consuming and require radioactively labelled antigen. With our SPR-based immunoassay the overall assay time is reduced by a factor of >100 (from 4 days to 50 min), while sensitivity is maintained at a level comparable to that offered by RIA. Finally, the assay was used in a screening study of newly diagnosed type 1 diabetes patients and non-diabetic subjects.

    List of papers
    1. Investigation of sera from various species by using lectin affinity arrays and scanning ellipsometry
    Open this publication in new window or tab >>Investigation of sera from various species by using lectin affinity arrays and scanning ellipsometry
    Show others...
    2005 (English)In: Analytica Chimica Acta, ISSN 0003-2670, E-ISSN 1873-4324, Vol. 530, no 2, p. 167-171Article in journal (Refereed) Published
    Abstract [en]

    Serum proteins of different species and of different human blood groups exhibit various protein glycosylation patterns. Sera from human, pig, sheep and guinea pig have been applied to a panel of eight different lectins immobilized on a gold wafer. The biorecognition has been evaluated with scanning ellipsometry and the two-dimensional matrices obtained have been treated with image analysis and MVDA for evaluation. The results showed a clear difference in protein binding pattern between the different species and thereby separation of the different sera could be made. Dendograms indicate that human and pig sera are the most related of the four different sera investigated.

    Keywords
    Serum proteins, lectins, scanning ellipsometry, image analysis, multivariate data analysis
    National Category
    Chemical Sciences
    Identifiers
    urn:nbn:se:liu:diva-12466 (URN)10.1016/j.aca.2004.09.022 (DOI)
    Available from: 2008-09-06 Created: 2008-09-06 Last updated: 2017-12-13Bibliographically approved
    2. Biosensor discrimination of meat juice from various animals using a lectin panel and ellipsometry
    Open this publication in new window or tab >>Biosensor discrimination of meat juice from various animals using a lectin panel and ellipsometry
    2005 (English)In: Analytica Chimica Acta, ISSN 0003-2670, E-ISSN 1873-4324, Vol. 547, no 2, p. 229-236Article in journal (Refereed) Published
    Abstract [en]

    In this work, simple microcontact printed gold-wafers were used to make a lectin panel for investigation and discrimination of different meat juices from fresh meat of cattle, chicken, pig, cod, turkey and lamb. Seven different lectins were thus attached to gold surfaces using the streptavidin–biotin method. Lectins recognize and bind specifically to carbohydrate structures present on different proteins. The biorecognition was evaluated with null ellipsometry and the data obtained was related to an internal standard of lactoferrin. The data was evaluated with multivariate data analysis techniques to identify possible discrimination or grouping of data. Scanning ellipsometry was used for visualization of the binding pattern of the lectins and the meat juice proteins. The two-dimensional images obtained could be used to visualize the protein distribution, furthermore, to exclude anomalies. The results showed that the different meat juices from the six different species: cattle, chicken, pig, cod, turkey and lamb could be discriminated from each other. The results showed to be more repetitive for the mammalian meat juices. Using a simple model based on an artificial neuronal net, it was also possible to classify meat juices from the mammals investigated.

    Keywords
    Lectin panel; Ellipsometry; Meat juice; Multivariate data analysis
    National Category
    Chemical Sciences
    Identifiers
    urn:nbn:se:liu:diva-12467 (URN)10.1016/j.aca.2005.05.054 (DOI)
    Available from: 2008-09-06 Created: 2008-09-06 Last updated: 2017-12-13Bibliographically approved
    3. Detection of global glycosylation changes of serum proteins in type 1 diabetes using a lectin panel and multivariate data analysis
    Open this publication in new window or tab >>Detection of global glycosylation changes of serum proteins in type 1 diabetes using a lectin panel and multivariate data analysis
    Show others...
    2008 (English)In: Talanta: The International Journal of Pure and Applied Analytical Chemistry, ISSN 0039-9140, E-ISSN 1873-3573, Vol. 76, no 2, p. 333-337Article in journal (Refereed) Published
    Abstract [en]

    Global glycosylation changes of serum proteins in type 1 diabetic patients have in this paper been investigated based on the interaction of the saccharide moiety of serum proteins with different lectins. Lectins are proteins, which bind carbohydrates specifically and reversibly. Panels with lectins of various carbohydrate specificities were immobilized on gold surfaces. Sera from healthy individuals, newly diagnosed type 1 diabetes patients and type 1 diabetes patients having had the disease for 4–6 years, respectively, were applied to the lectin panel. The biorecognition was evaluated with null ellipsometry. Data obtained were related to an internal standard of lactoferrin. Multivariate data analysis (MVDA) techniques were used to analyze data.

    Principal component analysis showed that the lectin panel enabled discrimination between sera from the three different above-mentioned groups. Using an artificial neuronal net (ANN), it was possible to correctly categorize unknown serum samples into one of the three groups.

     

    Keywords
    Lectin panel, Glycosylation changes, Type 1 diabetes, Ellipsometry, MVDA
    National Category
    Chemical Sciences
    Identifiers
    urn:nbn:se:liu:diva-12468 (URN)10.1016/j.talanta.2008.02.046 (DOI)
    Available from: 2008-09-06 Created: 2008-09-06 Last updated: 2017-12-13Bibliographically approved
    4. An indirect competitive immunoassay for insulin autoantibodies based on surface plasmon resonance
    Open this publication in new window or tab >>An indirect competitive immunoassay for insulin autoantibodies based on surface plasmon resonance
    Show others...
    2008 (English)In: Biosensors and Bioelectronics, ISSN 0956-5663, Vol. 24, no 4, p. 876-881Article in journal (Refereed) Published
    Abstract [en]

    We have developed a sensitive and specific method based on surface plasmon resonance (SPR) for detection of insulin autoantibodies (IAA) in serum samples from individuals at high risk of developing type 1 diabetes (T1D). When measuring trace molecules in undiluted sera with label-free techniques like SPR, non-specific adsorption of matrix proteins to the sensor surface is often a problem, since it causes a signal that masks the analyte response. The developed method is an indirect competitive immunoassay designed to overcome these problems. Today, IAA is mainly measured in radio immunoassays (RIAs), which are time consuming and require radioactively labeled antigen. With our SPR-based immunoassay the overall assay time is reduced by a factor of >100 (4 days to 50 min), while sensitivity is maintained at a level comparable to that offered by RIA.

    Keywords
    SPR, Type 1 diabetes, Insulin autoantibodies, Indirect competitive immunoassay, RIA
    National Category
    Other Basic Medicine
    Identifiers
    urn:nbn:se:liu:diva-12469 (URN)10.1016/j.bios.2008.07.018 (DOI)
    Note
    The status of article IV on the day of defence was: Accepted.Available from: 2008-09-06 Created: 2008-09-06 Last updated: 2018-01-13Bibliographically approved
    5. Determination of insulin autoantibodies using surface plasmon resonance: A screening study of newly diagnosed type 1 diabetes patients
    Open this publication in new window or tab >>Determination of insulin autoantibodies using surface plasmon resonance: A screening study of newly diagnosed type 1 diabetes patients
    Show others...
    2008 (English)Manuscript (preprint) (Other academic)
    Abstract [en]

    We have investigated the screening potential of a surface plasmon resonance (SPR)-based indirectcompetitive immunoassay for quantification of insulin autoantibodies (IAA) in sera from childrennewly diagnosed with type 1 diabetes (T1D), using a radioimmunoassay (RIA) as reference technique.The two methods agreed well with respect to sample classification of 54 sera from newly diagnosedT1D children and 32 reference sera from non-diabetic children. Interestingly, five samples from newlydiagnosed T1D patients classified as IAA-negative according to RIA were IAA-positive with the SPRbasedassay, suggesting that the SPR-based assay might provide a higher sensitivity than the referenceRIA. However, 14 percent of the analyzed samples (five samples from non-diabetics and seven fromnewly diagnosed T1D patients) gave rise to anomalously high and easily distinguishable responses withthe SPR-based method, precluding IAA-quantification. A considerable part of the paper is devoted to adiscussion of possible causes of these anomalous responses. They were not due to temporary changesin the status of the patients, such as infections at the time of sampling, and also not related tocomplement activation. It is speculated whether a plausible explanation should instead be sought in theexistence of anti-idiotypic antibodies to IAA.

    National Category
    Chemical Sciences
    Identifiers
    urn:nbn:se:liu:diva-12470 (URN)
    Available from: 2008-09-06 Created: 2008-09-06 Last updated: 2015-10-05Bibliographically approved
  • 3.
    Carlsson, Jenny
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics. Linköping University, The Institute of Technology.
    Surface analytical methods and multivariate data analysis applied to lectin panels2004Licentiate thesis, comprehensive summary (Other academic)
    Abstract [en]

    In this thesis lectin panels on gold wafers were utilized to investigate sera from different mammals and meat juices from various species of animals. Lectins, which are a group of diverse, natural proteins recognize and bind to different carbohydrate structures present on the sera proteins and on the proteins in the different meat juices. The binding patterns from the relatively unspecific interactions between lectins and carbohydrate structures were evaluated with techniques based on ellipsometry. The resulting data was treated with multivariate data analysis (MVDA) techniques, especially principal component analysis (PCA), to identify separation or grouping of data.

    It was shown that lectin panels combined with ellipsometric techniques and MVDA could be used to separate sera from different mammals and also a possible relation between species could be seen. Meat juices from the different species evaluated were also possible to separate and using a simple model based on an artificial neuronal net, it was also possible to classify meat juices from the mammals investigated. In spite of its great analytical potential, not much work has yet been done utilizing MVDA together with bioanalytical methods. The results in this thesis however, show great potential for combining lectin panels with MVDA.

    This work, regarding lectin panels, was incorporated as a part of a EU-project, Nanocell. The aim of the Nanocell-project was to develop a biosensor consisting of a single biomolecule electrically interfaced to nanoelectrodes, which is sensed electronically/optically.

    List of papers
    1. Investigation of sera from various species by using lectin affinity arrays and scanning ellipsometry
    Open this publication in new window or tab >>Investigation of sera from various species by using lectin affinity arrays and scanning ellipsometry
    Show others...
    2005 (English)In: Analytica Chimica Acta, ISSN 0003-2670, E-ISSN 1873-4324, Vol. 530, no 2, p. 167-171Article in journal (Refereed) Published
    Abstract [en]

    Serum proteins of different species and of different human blood groups exhibit various protein glycosylation patterns. Sera from human, pig, sheep and guinea pig have been applied to a panel of eight different lectins immobilized on a gold wafer. The biorecognition has been evaluated with scanning ellipsometry and the two-dimensional matrices obtained have been treated with image analysis and MVDA for evaluation. The results showed a clear difference in protein binding pattern between the different species and thereby separation of the different sera could be made. Dendograms indicate that human and pig sera are the most related of the four different sera investigated.

    Keywords
    Serum proteins, lectins, scanning ellipsometry, image analysis, multivariate data analysis
    National Category
    Chemical Sciences
    Identifiers
    urn:nbn:se:liu:diva-12466 (URN)10.1016/j.aca.2004.09.022 (DOI)
    Available from: 2008-09-06 Created: 2008-09-06 Last updated: 2017-12-13Bibliographically approved
    2. Separation of meat juice from various animals using a lectin panel and ellipsometry
    Open this publication in new window or tab >>Separation of meat juice from various animals using a lectin panel and ellipsometry
    (English)Manuscript (preprint) (Other academic)
    Abstract [en]

    In this work simple microcontact printed gold-wafers were used to make a lectin panel for investigation and separation of different meat juices from fresh meat of cattle, chicken, pig, cod, turkey and lamb. Seven different lectins were thus attached to gold surfaces using the streptavidin-biotin method. Lectins recognize and bind specifically to carbohydrate structures present on different proteins. The bio-recognition was evaluated with null ellipsometry and the data obtained was related to an internal standard of lactoferrin. The data was evaluated with multivariate data analysis techniques to identify possible separation or grouping of data. Scanning ellipsometry was used for visualization of the binding pattern of the lectins and the meat juice proteins. The 2-dimensional images obtained could be used to visualize the protein distribution, furthermore, to exclude anomalies. The results showed that the different meat juices could be separated from each other. Using a simple model based on an artificial neuronal net, it was also possible to classify meat juices from the mammals investigated.

    National Category
    Engineering and Technology
    Identifiers
    urn:nbn:se:liu:diva-100839 (URN)
    Available from: 2013-11-13 Created: 2013-11-13 Last updated: 2013-11-13
  • 4.
    Carlsson, Jenny
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics . Linköping University, The Institute of Technology.
    Gullstrand, Camilla
    Linköping University, Department of Clinical and Experimental Medicine, Pediatrics . Linköping University, Faculty of Health Sciences.
    Ludvigsson, Johnny
    Linköping University, Department of Clinical and Experimental Medicine, Pediatrics . Linköping University, Faculty of Health Sciences. Östergötlands Läns Landsting, Centre of Paediatrics and Gynecology and Obstetrics, Department of Paediatrics in Linköping.
    Lundström, Ingemar
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics . Linköping University, The Institute of Technology.
    Winquist, Fredrik
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics . Linköping University, The Institute of Technology.
    Detection of global glycosylation changes of serum proteins in type 1 diabetes using a lectin panel and multivariate data analysis2008In: Talanta: The International Journal of Pure and Applied Analytical Chemistry, ISSN 0039-9140, E-ISSN 1873-3573, Vol. 76, no 2, p. 333-337Article in journal (Refereed)
    Abstract [en]

    Global glycosylation changes of serum proteins in type 1 diabetic patients have in this paper been investigated based on the interaction of the saccharide moiety of serum proteins with different lectins. Lectins are proteins, which bind carbohydrates specifically and reversibly. Panels with lectins of various carbohydrate specificities were immobilized on gold surfaces. Sera from healthy individuals, newly diagnosed type 1 diabetes patients and type 1 diabetes patients having had the disease for 4–6 years, respectively, were applied to the lectin panel. The biorecognition was evaluated with null ellipsometry. Data obtained were related to an internal standard of lactoferrin. Multivariate data analysis (MVDA) techniques were used to analyze data.

    Principal component analysis showed that the lectin panel enabled discrimination between sera from the three different above-mentioned groups. Using an artificial neuronal net (ANN), it was possible to correctly categorize unknown serum samples into one of the three groups.

     

  • 5.
    Carlsson, Jenny
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics . Linköping University, The Institute of Technology.
    Gullstrand, Camilla
    Linköping University, Department of Clinical and Experimental Medicine, Pediatrics . Linköping University, Faculty of Health Sciences.
    Westermark, Gunilla
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Ludvigsson, Johnny
    Linköping University, Department of Clinical and Experimental Medicine, Pediatrics . Linköping University, Faculty of Health Sciences. Östergötlands Läns Landsting, Centre of Paediatrics and Gynecology and Obstetrics, Department of Paediatrics in Linköping.
    Enander, Karin
    Linköping University, Department of Physics, Chemistry and Biology, Sensor Science and Molecular Physics . Linköping University, The Institute of Technology.
    Liedberg, Bo
    Linköping University, Department of Physics, Chemistry and Biology, Sensor Science and Molecular Physics . Linköping University, The Institute of Technology.
    An indirect competitive immunoassay for insulin autoantibodies based on surface plasmon resonance2008In: Biosensors and Bioelectronics, ISSN 0956-5663, Vol. 24, no 4, p. 876-881Article in journal (Refereed)
    Abstract [en]

    We have developed a sensitive and specific method based on surface plasmon resonance (SPR) for detection of insulin autoantibodies (IAA) in serum samples from individuals at high risk of developing type 1 diabetes (T1D). When measuring trace molecules in undiluted sera with label-free techniques like SPR, non-specific adsorption of matrix proteins to the sensor surface is often a problem, since it causes a signal that masks the analyte response. The developed method is an indirect competitive immunoassay designed to overcome these problems. Today, IAA is mainly measured in radio immunoassays (RIAs), which are time consuming and require radioactively labeled antigen. With our SPR-based immunoassay the overall assay time is reduced by a factor of >100 (4 days to 50 min), while sensitivity is maintained at a level comparable to that offered by RIA.

  • 6.
    Carlsson, Jenny
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics. Linköping University, The Institute of Technology.
    Gullstrand, Camilla
    Linköping University, Department of Clinical and Experimental Medicine, Pediatrics. Linköping University, Faculty of Health Sciences.
    Westermark, Gunilla
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Ludvigsson, Johnny
    Linköping University, Department of Clinical and Experimental Medicine, Pediatrics. Linköping University, Faculty of Health Sciences. Östergötlands Läns Landsting, Center of Paediatrics and Gynaecology and Obstetrics, Department of Paediatrics in Linköping.
    Enander, Karin
    Linköping University, Department of Physics, Chemistry and Biology, Sensor Science and Molecular Physics. Linköping University, The Institute of Technology.
    Liedberg, Bo
    Linköping University, Department of Physics, Chemistry and Biology, Sensor Science and Molecular Physics. Linköping University, The Institute of Technology.
    Determination of insulin autoantibodies using surface plasmon resonance: A screening study of newly diagnosed type 1 diabetes patients2008Manuscript (preprint) (Other academic)
    Abstract [en]

    We have investigated the screening potential of a surface plasmon resonance (SPR)-based indirectcompetitive immunoassay for quantification of insulin autoantibodies (IAA) in sera from childrennewly diagnosed with type 1 diabetes (T1D), using a radioimmunoassay (RIA) as reference technique.The two methods agreed well with respect to sample classification of 54 sera from newly diagnosedT1D children and 32 reference sera from non-diabetic children. Interestingly, five samples from newlydiagnosed T1D patients classified as IAA-negative according to RIA were IAA-positive with the SPRbasedassay, suggesting that the SPR-based assay might provide a higher sensitivity than the referenceRIA. However, 14 percent of the analyzed samples (five samples from non-diabetics and seven fromnewly diagnosed T1D patients) gave rise to anomalously high and easily distinguishable responses withthe SPR-based method, precluding IAA-quantification. A considerable part of the paper is devoted to adiscussion of possible causes of these anomalous responses. They were not due to temporary changesin the status of the patients, such as infections at the time of sampling, and also not related tocomplement activation. It is speculated whether a plausible explanation should instead be sought in theexistence of anti-idiotypic antibodies to IAA.

  • 7.
    Carlsson, Jenny
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics . Linköping University, The Institute of Technology.
    Mecklenburg, Michael
    nanoArc Corp, Newport Beach, CA, USA.
    Lundström, Ingemar
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics . Linköping University, The Institute of Technology.
    Danielsson, Bengt
    Pure and Applied Biochemistry, Lund University, PO Box 124, SE-22100 Lund, Sweden .
    Winquist, Fredrik
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics . Linköping University, The Institute of Technology.
    Investigation of sera from various species by using lectin affinity arrays and scanning ellipsometry2005In: Analytica Chimica Acta, ISSN 0003-2670, E-ISSN 1873-4324, Vol. 530, no 2, p. 167-171Article in journal (Refereed)
    Abstract [en]

    Serum proteins of different species and of different human blood groups exhibit various protein glycosylation patterns. Sera from human, pig, sheep and guinea pig have been applied to a panel of eight different lectins immobilized on a gold wafer. The biorecognition has been evaluated with scanning ellipsometry and the two-dimensional matrices obtained have been treated with image analysis and MVDA for evaluation. The results showed a clear difference in protein binding pattern between the different species and thereby separation of the different sera could be made. Dendograms indicate that human and pig sera are the most related of the four different sera investigated.

  • 8.
    Carlsson, Jenny
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics. Linköping University, The Institute of Technology.
    Winquist, Fredrik
    Linköping University, Department of Physics, Chemistry and Biology, Biosensors and Bioelectronics. Linköping University, The Institute of Technology.
    Danielsson, Bengt
    Lund University, Lund, Sweden.
    Separation of meat juice from various animals using a lectin panel and ellipsometryManuscript (preprint) (Other academic)
    Abstract [en]

    In this work simple microcontact printed gold-wafers were used to make a lectin panel for investigation and separation of different meat juices from fresh meat of cattle, chicken, pig, cod, turkey and lamb. Seven different lectins were thus attached to gold surfaces using the streptavidin-biotin method. Lectins recognize and bind specifically to carbohydrate structures present on different proteins. The bio-recognition was evaluated with null ellipsometry and the data obtained was related to an internal standard of lactoferrin. The data was evaluated with multivariate data analysis techniques to identify possible separation or grouping of data. Scanning ellipsometry was used for visualization of the binding pattern of the lectins and the meat juice proteins. The 2-dimensional images obtained could be used to visualize the protein distribution, furthermore, to exclude anomalies. The results showed that the different meat juices could be separated from each other. Using a simple model based on an artificial neuronal net, it was also possible to classify meat juices from the mammals investigated.

  • 9.
    Carlsson, Jenny
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics . Linköping University, The Institute of Technology.
    Winquist, Fredrik
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics . Linköping University, The Institute of Technology.
    Danielsson, Bengt
    Pure and Applied Biochemistry, Lund University, SE-22 100 Lund, Sweden .
    Lundström, Ingemar
    Linköping University, Department of Physics, Chemistry and Biology, Applied Physics . Linköping University, The Institute of Technology.
    Biosensor discrimination of meat juice from various animals using a lectin panel and ellipsometry2005In: Analytica Chimica Acta, ISSN 0003-2670, E-ISSN 1873-4324, Vol. 547, no 2, p. 229-236Article in journal (Refereed)
    Abstract [en]

    In this work, simple microcontact printed gold-wafers were used to make a lectin panel for investigation and discrimination of different meat juices from fresh meat of cattle, chicken, pig, cod, turkey and lamb. Seven different lectins were thus attached to gold surfaces using the streptavidin–biotin method. Lectins recognize and bind specifically to carbohydrate structures present on different proteins. The biorecognition was evaluated with null ellipsometry and the data obtained was related to an internal standard of lactoferrin. The data was evaluated with multivariate data analysis techniques to identify possible discrimination or grouping of data. Scanning ellipsometry was used for visualization of the binding pattern of the lectins and the meat juice proteins. The two-dimensional images obtained could be used to visualize the protein distribution, furthermore, to exclude anomalies. The results showed that the different meat juices from the six different species: cattle, chicken, pig, cod, turkey and lamb could be discriminated from each other. The results showed to be more repetitive for the mammalian meat juices. Using a simple model based on an artificial neuronal net, it was also possible to classify meat juices from the mammals investigated.

  • 10.
    Masarova, J.
    et al.
    Masárová, J., Pure and Applied Biochemistry, LTH, Lund University, S-22100, Sweden, Institute of Chemistry, Slovak Academy of Sciences, SK-84238 Bratislava, Slovakia, Pure and Applied Biochemistry, LTH, Lund Univ., P.O. Box 124, S-22100, Lund, Sweden.
    Dey, E.S.
    Pure and Applied Biochemistry, LTH, Lund University, S-22100, Sweden.
    Carlsson, Jenny
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Applied Physics .
    Danielsson, B.
    Pure and Applied Biochemistry, LTH, Lund University, S-22100, Sweden.
    Novel peptide surface for reversible immobilization of concanavalin A2004In: Journal of Biochemical and Biophysical Methods, ISSN 0165-022X, E-ISSN 1872-857X, Vol. 60, no 2, p. 163-170Article in journal (Refereed)
    Abstract [en]

    Concanavalin A (Con A) was spontaneously adsorbed on polymyxin B surface. This peptide-lectin interaction was strong, KD=1.9×10 -10, based predominantly on creation of hydrophobic bonds, and was completely reversible. Concanavalin A on polymyxin B (PmB) retained higher binding capacity for yeast mannan, compared with covalently immobilized lectin. Kinetics of mannan-concanavalin A interaction were significantly different in dependence on type of concanavalin A immobilization. © 2004 Elsevier B.V. All rights reserved.

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