[用焦碳酸二乙酯对猪和鸡心脏胞质溶胶中天冬氨酸转氨酶的组氨酸残基进行修饰]
[Modification of histidine residues with diethylpyrocarbonate in aspartate transaminases from pig and chicken heart cytosol].
作者信息
Azarian A V, Mekhanik M L, Torchinskiĭ Iu M
出版信息
Biokhimiia. 1976 Nov;41(11):2075-7.
PMID:1022275
Abstract
One and three histidine residues react with diethylpyrocarbonate (DEP) at pH 6.5 in native aspartate transminases from cffect on the enzyme activity. The rest histidine residues in aspartate transaminases (approximately 6 in the chicken enzyme and 5 in the pig enzyme) are DEP-nonreactive and can be carbetoxylated only after protein denaturation. The presence of substrates does not affect the histidine modification in transaminases.
摘要
在来自鸡和猪的天然天冬氨酸转氨酶中，一个和三个组氨酸残基在pH 6.5的条件下与焦碳酸二乙酯（DEP）反应，这对酶活性有影响。天冬氨酸转氨酶中其余的组氨酸残基（鸡酶中约6个，猪酶中约5个）对DEP无反应，只有在蛋白质变性后才能被乙氧甲酰化。底物的存在不影响转氨酶中组氨酸的修饰。
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