Characterization of a mutant human erythrocyte carbonic anhydrase: carbonic anhydrase Ic-Guam. The amino acid substitution and carboxylesterase and hydratase activities.
Characterization of a mutant human erythrocyte carbonic anhydrase: carbonic anhydrase Ic-Guam. The amino acid substitution and carboxylesterase and hydratase activities.
复制标题
突变型人红细胞碳酸酐酶的表征：碳酸酐酶 Ic-Guam。
DOI：
10.1016/0003-9861(66)90419-x
复制
发表时间：
1966
影响因子：
3.9
通讯作者：
Y. S. Yu
中科院分区：
文献类型：
--
作者：
R. Tashian;S. Riggs;Y. S. Yu
证据表明，精氨酸残基取代了甘氨酸残基在异常的人红细胞碳酸酐酶，CA IcGuam。突变体的量的比率，以正常的酶分离的个体的溶血杂合的变异平均为0.56：1。正常碳酸酐酶和变异碳酸酐酶的羧酸酯酶比活力和CO2水合酶比活力无显著差异。
Evidence is presented which indicates that an arginine residue has substituted for a glycine residue in the abnormal human erythrocyte carbonic anhydrase, CA IcGuam. The ratio of the amount of mutant to normal enzyme isolated from hemolyzates of individuals heterozygous for the variant averaged 0.56:1. No significant differences were observed between the specific carboxylesterase activities or specific CO2hydratase activities of the normal and variant carbonic anhydrases.