Huang I Y, Rubinfien E, Yoshida A
J Biol Chem. 1980 Jul 10;255(13):6408-11.
As a part of the elucidation of the complete amino acid sequence of human phosphoglycerate kinase, 46 tryptic peptides, ranging in length from 1 to 26 residues, were isolated and characterized from the reduced and S-carboxymethylated enzyme. The isolated peptides were subjected to sequence analysis by the modified dansyl-Edman degradation procedure and automated Edman degradation technique. The results, together with the data on cyanogen bromide peptides and two additional tryptic peptides from cyanogen bromide peptides reported in the accompanying paper, established the complete amino acid sequence of human erythrocyte phosphoglycerate kinase.
作为阐明人磷酸甘油酸激酶完整氨基酸序列工作的一部分，从还原型和S-羧甲基化的该酶中分离并鉴定了46个胰蛋白酶肽段，其长度从1至26个残基不等。将分离得到的肽段通过改良的丹磺酰-埃德曼降解法和自动埃德曼降解技术进行序列分析。这些结果，连同在随附论文中报道的关于溴化氰肽段以及来自溴化氰肽段的另外两个胰蛋白酶肽段的数据，确定了人红细胞磷酸甘油酸激酶的完整氨基酸序列。
