Tabata N, Kazama H, Ohgi K, Irie M
Department of Microbiology, Hoshi College of Pharmacy, Tokyo, Japan.
Agric Biol Chem. 1991 Feb;55(2):461-9.
The complete primary structure of a nuclease from a Penicillium sp. [nuclease PA3 (Kazama et al., Chem. Pharm. Bull., 38, 3081 (1990)] was determined. The sequencing was done by analysis of the peptides generated by digestion of reduced and carboxymethylated nuclease PA3 (RCM nuclease PA3) with lysylendopeptidase, and by digestion with staphylococcal V8 protease or chemical cleavage with BrCN. It consisted of 270 amino acid residues and carbohydrate moieties attached to the 92nd, 138th, 184th, and 197th asparagine residues. The molecular weight of the protein moiety deduced from the sequence was 29,211. It contains four half cystine residues. The amino acid sequence was identical with that of P1 nuclease from Penicillium citrinum [K. Maekawa, S. Tsunasawa, G. Dibo, and F. Sakiyama, Abstracts of Papers, the 62nd Meeting of the Biochemical Society of Japan, Seikagaku, 61, 1013 (1989)] except that the 190th Thr residue was Ile in P1 nuclease.
确定了一种来自青霉菌的核酸酶的完整一级结构[核酸酶PA3(Kazama等人,《化学与药学通报》,38,3081(1990))]。测序是通过分析用赖氨酰内肽酶消化还原和羧甲基化的核酸酶PA3(RCM核酸酶PA3)产生的肽段,以及用葡萄球菌V8蛋白酶消化或用溴化氰进行化学裂解来完成的。它由270个氨基酸残基和连接在第92、138、184和197位天冬酰胺残基上的碳水化合物部分组成。从序列推导的蛋白质部分的分子量为29211。它含有四个半胱氨酸残基。该氨基酸序列与来自桔青霉的P1核酸酶的序列相同[K.前川、S.津名泽、G.迪博和F.崎山,《日本生物化学会第62届会议论文摘要》,《生物化学》,61,1013(1989)],只是P1核酸酶中第190位苏氨酸残基为异亮氨酸。