Anticoagulant Function of a 24-Kd Fragment Isolated From Human Fibrinogen Act Chains
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چکیده
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, -24,000 and contains an N-terminal sequence of met-glu-leu-glu-arg-pro-gly-glyasn-glu-ile. The fragment contains a large number of acidic amino acid residues, and its amino acid composition is similar to several fibrinogen Aa chains degradation fragments isolated previously. It corresponds to a peptide of the fibrinogen Aa chains, the N-terminal of which starts at a
منابع مشابه
Anticoagulant Function of a 24-Kd Fragment Isolated From Human Fibrinogen Act Chains
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, -24,000 and contains an N-terminal sequence of met-glu-leu-glu-arg-pro-gly-glyasn-glu-ile. The fragment contains a large number of acidic amino acid residues, and its amino acid composition is simila...
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تاریخ انتشار 2003