Purification and partial characterization of a D-like fragment from human fibrinogen, produced by human leukocyte elastase
article
Digestion of human fibrinogen with human leukocyte elastase in the presence of Ca2+ yields a D-like fragment of M(r) 93000. This fragment was purified by gel filtration on Sephacryl S-200 followed by chromatofocusing. The purified fragment was partially characterized and compared with a fragment termed D-cate, which is produced by plasmin digestion of fibrinogen in the presence of Ca2+. The molecular weights of the constituent chains of the D-like fragment and D-cate were similar. The D-like fragment precipitated with antisera directed against D-cate, but not with antisera against fragment E. The name D-elastase for the fragment is suggested. Differences between the D-elastase and D-cate fragments were found in amino-terminal amino acids, in isoelectric point and in the expression of D antigenic determinants. Two major functional differences were demonstrated: fragment D-elastase had a much stronger anticlotting potency than D-cate and the binding of Ca2+ by D-elastase and D-cate differed qualitatively and quantitatively. Since it has been suggested that the calcium-binding and anticlotting properties of D-cate and related to a carboxyl-terminal 13000 stretch of the ??-chain, the present findings for D-elastase indicate that the differences in these properties between D-cate and D-elastase are due to differences in this area of the molecule.
Chemicals/CAS: elastase, 9004-06-2; fibrinogen, 9001-32-5; Calcium, 7440-70-2; Fibrin Fibrinogen Degradation Products; fibrinogen D fragment; Fibrinogen, 9001-32-5; Pancreatic Elastase, EC 3.4.21.36
Chemicals/CAS: elastase, 9004-06-2; fibrinogen, 9001-32-5; Calcium, 7440-70-2; Fibrin Fibrinogen Degradation Products; fibrinogen D fragment; Fibrinogen, 9001-32-5; Pancreatic Elastase, EC 3.4.21.36
Topics
TNO Identifier
229357
ISSN
00063002
Source
Biochimica et Biophysica Acta, 755(2), pp. 300-306.
Pages
300-306
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