Abstract
In 1951, Bailey et al published the first direct evidence that thrombin acts as a protease in the conversion of fibrinogen to fibrin. Bettleheim and Bailey (1952) showed subsequently that thrombin catalyzes the hydrolysis of two peptides from the fibrinogen molecule. In addition, thrombin has been reported to attack casein ( Schultz and Schwick, 1951) and probably gelatin ( Kay, 1951). Guest and Ware (1950) found that thrombin, at a concentration 10,000 times that needed for coagulation, would dissolve fibrin. The lysis of fibrin by thrombin has been confirmed by Seegers and coworkers (1958) who used thrombin with the highest activity yet obtained, 4100 units per mg. Bailey and Bettleheim (1955) reported no effect on rabbit myosin or ovalbumin. Sherry and Troll (1954) have shown that thrombin catalyzes the hydrolysis of tosylarginine methyl ester. It has also been reported to hydrolyze lysine ethyl ester slowly ( Ehrenpreis et al, 1957). It appears that thrombin has a limited proteolytic activity with substrate requirements similar to trypsin but more specific. The present report showing a limited digestion of albumin by thrombin is part of a study to determine the possible usefulness of thrombin in studies of protein structure.
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