| Literature DB >> 16955961 |
R J Speer1, H Ridgway, J M Hill.
Abstract
An improved method for the isolation of highly purified active human Hageman factor has been described. An overall recovery of 25% with a purification of 10(6) has been achieved. Certain of the physical and chemical characteristics of XII have been elucidated. Selective chemical modification of functional groups and a variety of enzymatic assays have been employed in an effort to shed light on the mechanism of action of this procoagulant.Entities:
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Year: 1965 PMID： 16955961
Source DB: PubMed Journal: Thromb Diath Haemorrh ISSN： 0340-5338