A monoclonal antibody to human insulin-like growth factor-I: characterization, use in radioimmunoassay and effect on the biological activities of the growth factor
Autor: | A. T. Holder, A. Dabestani, D. J. Morrell, M. A Preece, A. M. Taylor, H. Dadi, J. More, C. R. Buchanan |
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Rok vydání: | 1989 |
Předmět: |
medicine.medical_specialty
medicine.drug_class medicine.medical_treatment Antibody Affinity Radioimmunoassay Cross Reactions Monoclonal antibody Mice Endocrinology Antibody Specificity Somatomedins Internal medicine medicine Animals Humans Insulin-Like Growth Factor I Molecular Biology Mice Inbred BALB C Hybridomas biology Insulin Growth factor Antibodies Monoclonal Biological activity Ovalbumin Polyclonal antibodies biology.protein Antibody |
Zdroj: | Journal of Molecular Endocrinology. 2:201-206 |
ISSN: | 1479-6813 0952-5041 |
DOI: | 10.1677/jme.0.0020201 |
Popis: | A monoclonal antibody (BPL-M23) to insulin-like growth factor-I (IGF-I) was obtained following immunization of BALB/c mice with human IGF-I conjugated to ovalbumin. The affinity constant of BPL-M23 for IGF-I was 10·5 litres/nmol and the cross-reactivities of IGF-II, multiplication-stimulating activity III-2 and insulin were 08, 003 and less than 0·0001 % respectively. Porcine, bovine, ovine and rabbit sera, but not rat or mouse sera, showed substantial reactivity with the antibody. Comparison of radioimmunoassay analyses of 54 human serum samples from normal subjects and acromegalic and GH-deficient patients using BPL-M23 and a polyclonal rabbit antiserum (R557A) to human IGF-I showed a high correlation, indicating the usefulness of the monoclonal antibody in radioimmunoassay. Monoclonal antibody BPL-M23 was capable of abolishing the sulphation, mitogenic and insulin-like activities of IGF-I in in-vitro bioassays, suggesting that these activities may rely upon the same receptor-binding site which is near to the antibody-binding site. |
Databáze: | OpenAIRE |
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