Some molecular and functional changes in high molecular weight kininogen induced by plasmin and trypsin
| Autor: | Jozef Kleniewski, Constance J. Wagner, Virginia H. Donaldson |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
Proteases
Protein Conformation Plasmin High-molecular-weight kininogen Size-exclusion chromatography Epitope Epitopes medicine Humans Streptokinase Trypsin Fibrinolysin Kininogens Chemistry Prekallikrein food and beverages Hematology Blood Coagulation Factors Molecular Weight Biochemistry Sephadex Chromatography Gel Electrophoresis Polyacrylamide Gel circulatory and respiratory physiology medicine.drug |
| Zdroj: | Thrombosis Research. 25:387-399 |
| ISSN: | 0049-3848 |
| DOI: | 10.1016/0049-3848(82)90129-3 |
| Popis: | When purified human HMW-kininogen was digested by plasmin, its specific antigenic properties were initially enhanced and then gradually destroyed, but its clot-promoting activity (Fitzgerald factor activity) was only slightly decreased. When endogenous serum plasminogen was activated by streptokinase, similar alterations in specific HMW-kininogen antigens and Fitzgerald factor activity occurred. In contrast, trypsin induced increased antigenic properties initially, but readily destroyed the Fitzgerald factor activity and less readily destroyed the specific HMW-kininogen antigenic properties in purified HMW-kininogen and in normal human serum. When normal serum was treated with streptokinase, the antigenic properties shared by HMW and LMW-kininogens were in Sephadex G-200 fractions of lower molecular weight than in the case of untreated serum, but the elution volumes of specific HMW-kininogen antigens and Fitzgerald factor activity were not significantly altered. When prekallikrein-deficient serum was subjected to the same G-200 gel filtration process, there was a broad overlap in the elution volumes of antigens shared by both HMW and LMW-kininogens with specific HMW-kininogen antigenic and coagulant properties, which remained after streptokinase treatment of the serum. Depsite the disparate rates of destruction of the antigenic and clot-promoting portion of HMW-kininogen by proteases these properties did not separate from one another during ion exchange chromatography. |
| Databáze: | OpenAIRE |
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