Meloun B, Baudys M, Pohl J, Pavlík M, Kostka V
Department of Biochemistry, Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Science, Prague.
J Biol Chem. 1988 Jul 5;263(19):9087-93.
The complete amino acid sequence of bovine spleen cathepsin B was determined by manual and automatic Edman degradation of fragments prepared by proteolytic or chemical digestion of the enzyme. The single-chain form of the enzyme consists of 253 amino acid residues and its Mr is 27,468 (carbohydrate moiety not included). The light chain (residues 1-47) and the heavy chain (residues 50-253) of the enzyme are linked by the sequence -Gly-Arg (residues 48 and 49) in the single-chain form. Bovine spleen cathepsin B shows 80% sequence homology with cathepsins B from other species. An outstanding feature of bovine spleen cathepsin B not observed with the other cathepsins B is the presence of two additional half-cystine residues.
通过对经酶解或化学消化制备的片段进行手动和自动的埃德曼降解,确定了牛脾组织组织蛋白酶B的完整氨基酸序列。该酶的单链形式由253个氨基酸残基组成,其相对分子质量为27,468(未包括碳水化合物部分)。该酶的轻链(第1至47位残基)和重链(第50至253位残基)以单链形式通过-Gly-Arg序列(第48和49位残基)相连。牛脾组织组织蛋白酶B与其他物种的组织蛋白酶B具有80%的序列同源性。牛脾组织组织蛋白酶B有一个其他组织蛋白酶B未观察到的显著特征,即存在另外两个半胱氨酸残基。