Rocha V, Deeley M, Crawford I P
J Bacteriol. 1979 Jan;137(1):700-3. doi: 10.1128/jb.137.1.700-703.1979.
Two labeled peptides were recovered from tryptic digests of the NaB3H4-reduced, performic acid-oxidized beta2 protein of Serratia marcescens tryptophan synthase. These two pyridoxyl peptides were identical except for the presence or absence of an NH2-terminal arginyl residue. Tryptic digestion of nonreduced, performic acid-oxidized protein allowed isolation of the peptides that comprise the two halves of the pyridoxyl peptide. The partial primary structure for this region of the protein was shown to be Arg-Glx-Asx-Ler-Leu-His(Gly,Gly,Ala,His)Lys(Pxy)-Thr-Asx-Glx-Val(Leu,Gly,Glx,Ala,Leu,Leu,Ala)Lys. All the data available indicate that the sequence is identical with the homologous region from the Escherichia coli enzyme.
从粘质沙雷氏菌色氨酸合成酶的NaB3H4还原、过甲酸氧化的β2蛋白的胰蛋白酶消化物中回收了两种标记肽。这两种吡哆醛肽除了存在或不存在NH2末端精氨酰残基外是相同的。对未还原、过甲酸氧化的蛋白进行胰蛋白酶消化，可以分离出构成吡哆醛肽两半的肽。该蛋白这一区域的部分一级结构显示为Arg-Glx-Asx-Ler-Leu-His(Gly,Gly,Ala,His)Lys(Pxy)-Thr-Asx-Glx-Val(Leu,Gly,Glx,Ala,Leu,Leu,Ala)Lys。所有可得数据表明该序列与大肠杆菌酶的同源区域相同。
