Answers are grounded in this paper and cite their sources.
A method for the purification of bovine thrombin (EC 3.4.4.13) from Parke-Davis topical thrombin is described. The purified preparation has a constant specific activity although it has previously been shown to contain at least two enzymatically active proteins of similar molecular weights and amino acid composition. The average molecular weight of this purified material as determined by gel filtration, sedimentation equilibrium, and reaction with 14C-diisopropyl-fluorophosphate is shown to be close to 34,000. The carbohydrate content of the purified material is approximately 10% of the protein content, but evidence is presented that this carbohydrate is probably an artifact of the purification procedure. The amino acid composition of the purified thrombin is reported based upon an assumed molecular weight of 34,000.
No takes yet. Share an insight, caveat, or question.
Batt et al. (1970) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: