Abstract
A method is described for obtaining purified bovine thrombin by chromatography on phosphate cellulose, and purified bovine prothrombin by chromatography on diethylaminoethyl cellulose. Both proteins are obtained as single components, and in high yield. The purified prothrombin does not convert to thrombin in 25% sodium citrate solution or protamine sulphate solution. The N-terminal amino acid is the same as in purified prothrombin obtained by different methods in this laboratory, but instead of tyrosine and glycine the C-terminal amino acid is serine. A fundamental difference in structure is thus associated with altered activation characteristics.
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 callDisclaimer: 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.
