Year: 1977
Type: conference-paper
Abstract: Fibrinoligase (thrombin and calcium activated factor XIII) from human plasma catalyzes the incorporation of dansylcadaverine and 14C-putrescine into myosin and actin prepared from either human platelets or rabbit skeletal muscle. An average of 3 to 4 moles of amine are incorporated per mole of myosin of either type when the enzyme is used under saturating conditions. The rate of incorporation is 1.4 to 2 fold faster for filamentous than for soluble myosin. Electrophoretic analysis on Polyacrylamide and agarose gels in the presence of sodium dodecyl sulfate and 2-mercaptoethanol was used for locating the acceptor sites and for the detection of possible cross-links. Both heavy and light chains of platelet as well as muscle myosin incorporate dansylcadaverine and 14C-putrescine. However, in quantitative terms, the incorporation into the light chains of either type is only a small fraction of that incorporated into the heavy chains. Fibrinoligase also catalyzes the formation of highly cross-linked polymers in both myosin and actin (platelet or muscle) indicating the presence of acceptor and donor sites in the two contractile proteins.
Source: Thrombosis and Haemostasis
Institution: Northwestern University
Language: English
Subfield: Pulmonary and Respiratory Medicine
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
OpenAlex ID: W2945700254