Abstract
Abstract Preparations of bovine thrombin (EC 3.4.4.13) have been separated into various fractions by means of chromatographic methods including gradient-elution chromatography on DEAE-Sephadex A-25, a DEAE derivative of dextran. The specific clotting activity has thereby been increased 5-fold to a value of 256 NIH units/mg dry wt. with a recovery of 60% of the clotting activity. A fibrinolytic component has also been separated and isolated under conditions of extended dialysis or repeated freeze-drying. The activity of this component is about 200–400 times as high as the fibrinolytic activity of the initial thrombin preparation with a recovery on a weight basis amounting to 6–12% only. The fibrinolytic activity in the starting material thus appears to be masked or to be present in the form of a precursor, from which it is generated under certain conditions. Fibrinolytic activity is inhibited by chromatographically pure thrombin, this effect being increased by another of the fractions obtained. Compared to the purest of thrombin preparations as obtained by Seegers et al. the thrombin fractions here reported still represent an enzyme of 10–13% purity only. The fibrinolytic activity of chromatographically homogeneous thrombin preparations (clotting thrombin) is believed to be nil or extremely low.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
