| Autor: |
Björk I, Larsson LJ, Lindblom T, Raub E |
| Jazyk: |
angličtina |
| Zdroj: |
The Biochemical journal [Biochem J] 1984 Jan 01; Vol. 217 (1), pp. 303-8. |
| DOI: |
10.1042/bj2170303 |
| Abstrakt: |
The stoichiometry of the individual steps, i.e. polypeptide chain cleavage, hydrolysis of the putative thioester bond and conformational change, of the reaction between alpha 2-macroglobulin and trypsin or chymotrypsin was analysed. The chain cleavage was monitored by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, the thioester hydrolysis by both a spectroscopic and a fluorimetric technique and the conformational change by tryptophan fluorescence. A stoichiometry of close to 2:1 was obtained for all reactions. This finding indicates that the alpha 2-macroglobulin half-molecule is an independent functional unit of the inhibitor, within which co-operativity between the two subunits may occur. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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