Fibrin polymerization studied by static and dynamic light-scattering as a function of fibrinopeptide A release

✍ Scribed by P. Wiltzius; G. Dietler; W. Känzig; A. Häberli; P. W. Straub

• Publisher: Wiley (John Wiley & Sons)
• Year: 1982
• Tongue: English
• Weight: 895 KB
• Volume: 21
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360211109

✦ Synopsis

Abstract

The polymerization of fibrin induced by the enzyme thrombin was investigated in the pregelation phase by combining measurements of the release of the fibrinopeptides A with static and dynamic light‐scattering at scattering angles ranging from 5°–150°. Without making any assumptions about the polymer distribution, one is led to the following conclusions: The aggregates are rodlike; the Flory‐Stockmayer model is to be preferred over the percolation model, i.e., cyclic bonds are infrequent; in the early stages the experiments indicate a functionality f = 2 (number of reactive binding sites per monomer) that increases with increasing release of fibrinopeptides A, eventually approaching the value f = 4; the number of binding sites involved in a bond is about twice the number of the released fibrinopeptides A; and in the polymers the monomer units aggregate end‐to‐end in the very early stage and then in a staggered overlap.