Ambler R P
Biochem J. 1975 Nov;151(2):197-218. doi: 10.1042/bj1510197.
The amino acid sequence of the penicillinase (penicillin amido-beta-lactamhydrolase, EC 3.5.2.6) from Staphylococcus aureus strain PC1 was determined. The protein consists of a single polypeptide chain of 257 residues, and the sequence was determined by characterization of tryptic, chymotryptic, peptic and CNBr peptides, with some additional evidence from thermolysin and S. aureus proteinase peptides. A mistake in the preliminary report of the sequence is corrected; residues 113-116 are now thought to be -Lys-Lys-Val-Lys- rather than -Lys-Val-Lys-Lys-. Detailed evidence for the amino acid sequence has been deposited as Supplementary Publication SUP 50056 (91 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1975) 145, 5.
测定了金黄色葡萄球菌PC1菌株青霉素酶(青霉素酰胺-β-内酰胺水解酶,EC 3.5.2.6)的氨基酸序列。该蛋白质由一条含257个残基的单多肽链组成,其序列通过对胰蛋白酶、胰凝乳蛋白酶、胃蛋白酶和溴化氰肽段的表征来确定,同时还有来自嗜热菌蛋白酶和金黄色葡萄球菌蛋白酶肽段的一些补充证据。序列初步报告中的一个错误已得到纠正;现在认为第113 - 116位残基是-Lys-Lys-Val-Lys-,而不是-Lys-Val-Lys-Lys-。氨基酸序列的详细证据已作为补充出版物SUP 50056(91页)存放在英国西约克郡韦瑟比波士顿温泉市英国国家图书馆(出借部),邮编LS23 7BQ,可按《生物化学杂志》(1975年)第145卷第5期给出的条件从该处获取复印件。