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- W2069211545 abstract "Crystals of carboxypeptidase A were cross-linked with glutaraldehyde, and samples of the enzyme and apoenzyme were examined by thermogravimetric, dif- ferential thermal and thermomechanical analyses. Further samples were heat-treated under vacuum for various lengths of time, and examined by thermal analysis. Enzymatic activities were measured using the substrate carbobenzoxy-glycyl-L-phenyl- alanine. It proved possible to put forward explanations for all the phenomena observed, and in particular to identify the peak obtained due to loss of water from the zinc ion situated at the active site of the enzyme. The great stability of the cross- linked crystals, which had previously been commented on, was confirmed and the importance of water as a stabilising factor was indicated." @default.
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- W2069211545 date "1974-04-01" @default.
- W2069211545 modified "2023-09-25" @default.
- W2069211545 title "A thermal investigation of the stability of crystalline cross-linked carboxypeptidase a" @default.
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- W2069211545 doi "https://doi.org/10.1016/0040-6031(74)85114-2" @default.
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