Wade R D, Hass G M, Kumar S, Walsh K A, Neurath H
Department of Biochemistry, University of Washington, Seattle 98195.
Biochimie. 1988 Sep;70(9):1137-42. doi: 10.1016/0300-9084(88)90178-2.
The amino acid sequence of the activation peptide of bovine pro-carboxypeptidase A subunit I has been determined by automated Edman degradation of the cyanogen bromide fractions derived from the precursor protein. The activation peptide contains 94 amino acid residues in a unique sequence which precedes directly the amino-terminal alanine residue of carboxypeptidase A alpha. A notable feature of the activation peptide is the presence of acidic amino acid residues immediately preceding the site of activation. The amino acid sequence of the activation peptide of bovine pro-carboxypeptidase A shows extensive similarity to those of the corresponding porcine and rat enzymes.
通过对源自前体蛋白的溴化氰片段进行自动埃德曼降解，已确定了牛羧肽酶原A亚基I激活肽的氨基酸序列。该激活肽含有94个氨基酸残基，其独特序列直接位于羧肽酶Aα氨基末端丙氨酸残基之前。激活肽的一个显著特征是在激活位点之前紧邻存在酸性氨基酸残基。牛羧肽酶原A激活肽的氨基酸序列与相应的猪和大鼠酶的氨基酸序列具有广泛的相似性。
