Structural changes of subunit polypeptides of bovine fibrinogen during proteolysis
- 8 January 1974
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 336 (1), 86-99
- https://doi.org/10.1016/0005-2795(74)90387-0
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- A simple, large scale method for preparation of plasminogen-free fibrinogenThrombosis Research, 1972
- TITRATION OF THE ACCEPTOR CROSS‐LINKING SITES IN FIBRIN*Annals of the New York Academy of Sciences, 1972
- Microcrystals of a Modified FibrinogenNature, 1972
- A structural aspect of human fibrinogen suggested by its plasmin degradationFEBS Letters, 1971
- Rapid method for the purification of bovine thrombin and the inhibition of the purified enzyme with phenylmethylsulfonyl fluorideBiochemistry, 1971
- Crosslinking of human fibrin: Evidence for intermolecular crosslinking involving α‐chainsFEBS Letters, 1971
- Plasminogen: Purification from Human Plasma by Affinity ChromatographyScience, 1970
- Polypeptide chain involved in the cross-linking of stabilized bovine fibrinBiochemical and Biophysical Research Communications, 1970
- Digestion of fibrinogen by trypsin: II. Characterization of the large fragment obtainedBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963
- Digestion of fibrinogen by trypsin: I. Kinetic studies of the reactionBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963