Aggregation of fibrinogen molecules by metal ions |
| |
Authors: | F.S. Steven M.M. Griffin B.S. Brown T.P. Hulley |
| |
Affiliation: | Department of Medical Biochemistry, Stopford Building, University of Manchester, Manchester M13 9PT, UK |
| |
Abstract: | The ability of metal ions to cause physical aggregation of neutral solutions of bovine fibrinogen has been studied. Three categories were found: (a) ions (such as Ca2+, Mg2+ and Mn2+) which did not cause aggregation even when present in 1–100 mm concentrations: (b) ions (such as Fe2+, Cu2+ and Ni2+) which caused aggregation in the 0–10 mm concentration range, (c) ions (such as Hg2+, Zn2+, Cr3+, La3+) which caused aggregation in the 0–1000 μm concentration range. Aggregation occurs immediately the metal ion is brought into contact with the fibrinogen, and product formation reaches a steady state within 5 min. With the exception of Zn2+, all the ions that caused aggregation exhibited a threshold concentration below which no observable aggregation took place. The threshold concentration for Hg2+, the most effective ion studied, was 6 μm. Addition of excess EDTA caused resolubilization of the aggregated fibrinogen due to removal of the metal ions. Aggregation is thus thought to be a physical process initiated by binding of metal ions to those carboxyl groups in fibrinogen responsible for keeping the monomers apart in solution. The aggregation does not involve prior proteolytic degradation of the fibrinogen. |
| |
Keywords: | Fibrin fibrinogen aggregation metal ions |
本文献已被 ScienceDirect 等数据库收录! |
|