Rocha V, Brennan E F
J Bacteriol. 1980 May;142(2):729-31. doi: 10.1128/jb.142.2.729-731.1980.
Escherichia coli and Serratia marcescens tryptophan synthase beta 2 protein (EC 4.2.1.20) was subjected to mild trypsin proteolysis. Two separate folding regions (domains) of the E. coli (EF1 and EF2) and the S. marcescens (SF1 and SF2) enzyme were shown to form interspecies hybrid reconstituted molecules [(EF1-SF2)2 and (SF1-EF2)2] and intraspecies reconstituted molecules [(EF1-EF2)2 and (SF1-SF2)2] with equal efficiency. The data suggest that structural regions, associated with beta monomer assembly, exist somewhere on the domain fragments and that these regions are conserved.
对大肠杆菌和粘质沙雷氏菌的色氨酸合成酶β2蛋白（EC 4.2.1.20）进行温和的胰蛋白酶水解。结果表明，大肠杆菌（EF1和EF2）和粘质沙雷氏菌（SF1和SF2）酶的两个独立折叠区域（结构域）能够以相同效率形成种间杂交重组分子[（EF1-SF2）2和（SF1-EF2）2]以及种内重组分子[（EF1-EF2）2和（SF1-SF2）2]。这些数据表明，与β单体组装相关的结构区域存在于结构域片段的某个位置，并且这些区域是保守的。
