Murai H, Hara S, Ikenaka T, Oda K, Murao S
J Biochem. 1985 Jan;97(1):173-80. doi: 10.1093/oxfordjournals.jbchem.a135041.
Streptomyces Metallo-Proteinase Inhibitor (S-MPI) consists of 102 amino acid residues, including one methionine and two disulfide bridges. The complete amino acid sequence of S-MPI, including two disulfide bridges, was determined by sequencing of tryptic and chymotryptic peptides of two fragments obtained by cyanogen bromide cleavage followed by reduction and S-pyridylethylation of the protein. Incubation of the inhibitor with thermolysin slowly cleaved one peptide bond, Cys(64)-Val(65), which might be a reactive site of S-MPI.
链霉菌金属蛋白酶抑制剂(S-MPI)由102个氨基酸残基组成,包括一个甲硫氨酸和两个二硫键。通过对溴化氰裂解后经还原和S-吡啶基乙基化处理的蛋白质的两个片段的胰蛋白酶和胰凝乳蛋白酶肽段进行测序,确定了包括两个二硫键的S-MPI的完整氨基酸序列。该抑制剂与嗜热菌蛋白酶一起温育会缓慢裂解一个肽键,即半胱氨酸(64)-缬氨酸(65),这可能是S-MPI的一个活性位点。