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HK Lau
Division of Hematology, St. Michael's Hospital, Toronto, Ontario, Canada.
A fibrinogen fragment obtained by limited-plasmin proteolysis has been
isolated and purified to apparent homogeneity by gel filtrations. This
fragment, denoted as 24-Kd fragment, has an apparent M(r) approximately
24,000 and contains an N-terminal sequence of met-glu-leu-glu-arg-pro-
gly-gly-asn-glu-ile. The fragment contains a large number of acidic amino
acid residues, and its amino acid composition is similar to several
fibrinogen A alpha chains degradation fragments isolated previously. It
corresponds to a peptide of the fibrinogen A alpha chains, the N-terminal
of which starts at alpha Met-240. This peptide delays thrombin plasma
clotting time. It does not bind calcium ions and does not inhibit
thrombin's amidolytic activity. It binds to immobilized fibrin but not
fibrinogen. It also inhibits the polymerization of desAA and desAABB fibrin
monomers by simultaneously decreasing the maximum rate and the maximum
level of the polymerization reaction. However, the initial lag period of
this reaction is not affected by the fragment.
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| Copyright © 1993 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
