Subunits and susceptibility of fibrins formed from bovine fibrinogen by arvin, reptilase, thrombin and staphylothrombin

Subunits and susceptibility of fibrins formed from bovine fibrinogen by arvin, reptilase, thrombin and staphylothrombin

The rates of proteolysis by SKPL of 125I-bovine fibrins were compared depending on the enzyme used for fibrinogen - fibrin conversion and found to diminish in order: Reptilase, Arvin, thrombin and staphylothrombin. A∝ chain of bovine fibrinogen was shown to be degraded during incubation (24 hr) with...

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Veröffentlicht in:Thrombosis research 1975-04, Vol.6 (4), p.337-344
Hauptverfasser: Zajdel, M., Wȩgrzynowicz, Z., Sawecka, J., Kopeć, M.
Format: Artikel
Sprache:eng
Schlagworte:
Ancrod - pharmacology
Animals
Batroxobin - pharmacology
Cattle
Coagulase - pharmacology
Electrophoresis, Agar Gel
Endopeptidases - pharmacology
Fibrin - analysis
Fibrin - metabolism
Fibrinogen - analysis
Fibrinolysis - drug effects
Iodine Radioisotopes
Peptide Hydrolases - pharmacology
Plasminogen - pharmacology
Prothrombin - pharmacology
Streptokinase - pharmacology
Thrombin - pharmacology
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Zusammenfassung:The rates of proteolysis by SKPL of 125I-bovine fibrins were compared depending on the enzyme used for fibrinogen - fibrin conversion and found to diminish in order: Reptilase, Arvin, thrombin and staphylothrombin. A∝ chain of bovine fibrinogen was shown to be degraded during incubation (24 hr) with Reptilase or Arvin. A fraction of about 27,000 daltons was detected by SDS electrophoresis among the products of degradation of A∝ chain of bovine fibrin by Reptilase while no electrophoretically detectable fragments were formed by Arvin. The results demonstrate substantial differences in the action of Reptilase and Arvin on bovine and human fibrinogen.
ISSN:0049-3848
1879-2472
DOI:10.1016/0049-3848(75)90083-3