高活性马红细胞碳酸酐酶的序列：N端多态性（乙酰化丝氨酸/乙酰化苏氨酸）以及与类似哺乳动物同工酶的同源性。
Sequence of the high-activity equine erythrocyte carbonic anhydrase: N-terminal polymorphism (acetyl-Ser/acetyl-Thr) and homologies to similar mammalian isozymes.
作者信息
Jabusch J R, Deutsch H F
出版信息
Biochem Genet. 1984 Apr;22(3-4):357-67. doi: 10.1007/BF00484234.
PMID:6428393
Abstract
The amino acid sequence of the high-activity equine erythrocyte carbonic anhydrase (CA-II) has been determined. Two different N-termini are noted, the C1 form having an N-acetyl-serine and the C2 form an N-acetyl-threonine. The sequence of the equine enzyme is most homologous to the human CA-II isozyme, with 224 of the 259 residues being identical.
摘要
高活性马红细胞碳酸酐酶（CA-II）的氨基酸序列已被确定。发现有两种不同的N端，C1形式的N端为N-乙酰丝氨酸，C2形式的N端为N-乙酰苏氨酸。马酶的序列与人类CA-II同工酶的同源性最高，259个残基中有224个相同。
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