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Crotalus adamanteus 의 L - Amino Acid Oxidase 의 열로 인한 불활성에 대한 식초산염의 보호작용 기전
백운기,김상덕 ( Woon Ki Paik,San Gduk Kim ) 생화학분자생물학회 1975 BMB Reports Vol.8 No.3
The mechanism of the protective action of acetate against heat-inactivation of the L-amino acid oxidase (L-amino acid:oxygen oxidoreductase (deaminating, EC 1.4.3.2) of Crotalus adamanteus venom has been investigated. The entropy of activation for the heat-inactivation of the enzyme in the presence of acetate was 224 e.u. compared to 114 e.u. in its absence. The Km value of the enzyme for L-arginine was decreased from 3. 86 mM to 0. 77 mM in the presence of 330mM acetate. The Vmax was reduced from 227 to 161 ㎕O₂ consumed per hour per ㎎ of enzyme protein. These results are taken to mean that the protective action of acetate is by preventing the enzyme protein from assuming a less ordered state, at high pH, by combining at a site different from the substrate-binding site.