Effects of crosslinking on the rigidity and proteolytic susceptibility of human fibrin clots

Journal Article · Sun May 01 04:00:00 EDT 1983 · Thromb. Res.; (United States)

DOI:https://doi.org/10.1016/0049-3848(83)90081-6· OSTI ID:5515474

Gladner, J A; Nossal, R

Clots formed in reconstituted human plasma or from purified human fibrin were studied in order to assess the effects of subunit crosslinking on clot strength and on resistance to plasmin degradation. The relative amounts of alpha chain and gamma chain ligation were varied by adding factor XIII to the samples. We observe, as have others, that appreciable gamma-gamma crosslinking always precedes detectable formation of alpha dimer or alpha polymer. Non-invasive light scattering measurements of the shear modulus G(t) indicate that ligation of gamma chains and of alpha chains have qualitatively similar effects on clot strength. Since alpha crosslinking occurs very slowly in the clots which are formed from plasma, we infer that under physiological conditions the involvement of alpha chains in the development of clot strength probably is only a secondary function. Light scattering techniques also were used to study the size of particles shed from the surfaces of fibrin clots undergoing fibrinolysis, and no differences could be discerned as resulting from ligation of alpha chains.

• Research Organization: Laboratory of Biochemical Pharmacology, National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases, Bethesda, MD
• OSTI ID: 5515474
• Journal Information: Thromb. Res.; (United States), Journal Name: Thromb. Res.; (United States) Vol. 30:3; ISSN THBRA
• Country of Publication: United States
• Language: English

Related Subjects

550900* -- Pathology
59 BASIC BIOLOGICAL SCIENCES
BIOLOGICAL MATERIALS
BLOOD
BLOOD COAGULATION
BLOOD PLASMA
BODY FLUIDS
CHEMICAL REACTIONS
COAGULANTS
DECOMPOSITION
DRUGS
FIBRIN
FIBRINOLYSIS
HEMATOLOGIC AGENTS
HEMOSTATICS
MATERIALS
ORGANIC COMPOUNDS
PROTEINS
PROTEOLYSIS
SCLEROPROTEINS