Kallikrein modification with affinity to IgG present in higher amounts than normal in plasma from patients with Crohn's disease
| Autor: | S. Johannesen, Kjell Briseid |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
medicine.drug_class
Clinical Biochemistry Antibody Affinity Monoclonal antibody Amidohydrolases Crohn Disease Mole Blood plasma medicine Humans Factor XI Plasma Kallikrein Immunoassay chemistry.chemical_classification Crohn's disease Prekallikrein General Medicine Kallikrein medicine.disease Molecular biology Pathophysiology Enzyme chemistry Immunoglobulin G Factor XII Immunology Electrophoresis Polyacrylamide Gel |
| Zdroj: | Scandinavian Journal of Clinical and Laboratory Investigation. 63:425-430 |
| ISSN: | 1502-7686 0036-5513 |
| DOI: | 10.1080/00365510310002608 |
| Popis: | This study presents immunological and functional evidence to suggest that the activation of prekallikrein (PK) in human plasma yields two modifications of kallikrein. One of these modifications showed amidolytic properties strongly deviating from those registered for the main part of the enzyme. The substrates were S-2302, Bz-Pro-Phe-Arg-pNA, S-2366 and S-2222. In PAGE immunoblots the PK heavy chain mAb 13G11 was found to detect the kallikrein 85 kD double band and bands with mol. weights of about 152 and 135 kD. Such a 152 kD band could be removed together with an IgG fraction on a Protein G column. In this study the kallikrein identity was confirmed by an estimation of the levels obtained in amidolytic assays of mixtures of normal plasma and plasma deficient in FXI, which in immunological assays showed a PK level of 140-150%, of normal. A comparison in amidolytic assays of normal plasma and plasma from patients with Crohn's disease showed that patients' plasma contained a significantly higher level than normal of modified kallikrein. An IgG removal procedure removed all modified kallikrein, and did not affect ordinary kallikrein levels. |
| Databáze: | OpenAIRE |
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