Structure-function relationships in human α- and γ-thrombins

✍ Scribed by Lawrence J. Berliner

• Book ID: 104670200
• Publisher: Springer
• Year: 1984
• Tongue: English
• Weight: 847 KB
• Volume: 61
• Category: Article
• ISSN: 0300-8177
• DOI: 10.1007/bf00222493

✦ Synopsis

Human pro-coagulant alpha-thrombin may be proteolyzed under controlled conditions to the non-coagulant beta- and gamma-thrombin forms. These derivative forms nonetheless retain esterase and amidase activities with small substrates as well as several other thrombin functions. Structurally, human gamma-thrombin consists of three non-covalently associated fragments which retain structural integrity as measured by several spectroscopic criteria as well as enzymatic function. The protein folding characteristics of three-chain gamma-thrombin indicate that each fragment (domain) contains sufficient information to result in a correct renaturation of protein conformation. Those subtle structural differences which distinguish gamma- from alpha-thrombin are most likely the obstructions to fibrinogen binding which account for the loss of clotting activity.