Descalzi-Cancedda F, Caruso C, Romano M, di Prisco G, Camardella L
Biochem Biophys Res Commun. 1984 Jan 13;118(1):332-8. doi: 10.1016/0006-291x(84)91105-7.
Human erythrocyte glucose-6-phosphate dehydrogenase was purified to homogeneity by a simplified procedure, consisting of 2',5'-ADP-Sepharose affinity chromatography, followed by Sephadex G-100 gel filtration. The carboxy-terminal region of the protein was identified by carboxypeptidase digestion: the sequence -Lys-Leu-COOH was found instead of the reported -Gly-COOH, thus showing identity with the carboxy-terminal sequence of glucose-6-phosphate dehydrogenase from human leukocytes and platelets. In addition, the carboxyl-terminal peptide was isolated from a tryptic digest of the protein and sequenced. The sequence is: Trp-Val-Asp-Pro-His-Lys-Leu.
通过一种简化程序将人红细胞葡萄糖-6-磷酸脱氢酶纯化至同质,该程序包括2',5'-ADP-琼脂糖亲和层析,随后进行葡聚糖凝胶G-100凝胶过滤。通过羧肽酶消化鉴定了该蛋白质的羧基末端区域:发现序列为-Lys-Leu-COOH,而不是报道的-Gly-COOH,因此显示与人白细胞和血小板中的葡萄糖-6-磷酸脱氢酶的羧基末端序列相同。此外,从该蛋白质的胰蛋白酶消化物中分离出羧基末端肽并进行测序。序列为:Trp-Val-Asp-Pro-His-Lys-Leu。