Akparov V Kh, Belianova L P, Baratova L A, Stepanov V M
Biokhimiia. 1979 May;44(5):886-91.
Subtilisin 72, a serine proteinase secreted by Bac. subtilis strain 72 was purified by covalent chromatography on Sepharose sorbent containing p-(omega-aminomethyl)phenylboronic acid as a ligand. The homogeneity of subtilisin 72 was confirmed by isoelectrofocusing in a thin layer of polyacrylamide gel (pl 8.6). The amino acid composition of this enzyme is different from that of other subtilisins, e. g. subtilisin Carlsberg. The N = terminal amino acid sequence of subtilisin 72 traced up to the 35th residue turned to be the same as that of subtilisin Carlsberg with the exception of the 21st (Tyr) and the 30th (Ile) residues. This very pronounced extent of homology shows that subtilisin 72 is very similar although not identical to subtilisin Carlsberg.
枯草杆菌蛋白酶72是由枯草芽孢杆菌菌株72分泌的一种丝氨酸蛋白酶,通过在含有对(ω-氨基甲基)苯硼酸作为配体的琼脂糖吸附剂上进行共价层析进行纯化。通过在聚丙烯酰胺凝胶薄层中进行等电聚焦(pH值8.6)证实了枯草杆菌蛋白酶72的同质性。这种酶的氨基酸组成与其他枯草杆菌蛋白酶不同,例如卡尔伯格枯草杆菌蛋白酶。追溯到第35个残基的枯草杆菌蛋白酶72的N末端氨基酸序列,除了第21个(酪氨酸)和第30个(异亮氨酸)残基外,与卡尔伯格枯草杆菌蛋白酶的序列相同。这种非常显著的同源程度表明,枯草杆菌蛋白酶72与卡尔伯格枯草杆菌蛋白酶非常相似,尽管并不完全相同。