Ritonja A, Popović T, Kotnik M, Machleidt W, Turk V
Department of Biochemistry, J. Stefan Institute, Ljubljana, Yugoslavia.
FEBS Lett. 1988 Feb 15;228(2):341-5. doi: 10.1016/0014-5793(88)80028-0.
The complete amino acid sequences of human kidney cathepsin H (EC 3.4.22.16) and human kidney cathepsin L (EC 3.4.22.15) were determined. Cathepsin H contains 230 residues and has an Mr of 25116. The sequence was obtained by sequencing the light, heavy and mini chain and the peptides produced by cyanogen bromide cleavage of the single-chain form of the enzyme. The glycosylated mini chain is a proteolytic fragment of the propeptide of cathepsin H. Human cathepsin L has 217 amino acid residues and an Mr of 23720. Its amino acid sequence was deduced from N-terminal sequences of the heavy and light chains and from the sequences of cyanogen bromide fragments of the heavy chain. The fragments were aligned by comparison with known sequences of cathepsins H and L from other species. Cathepsins H and L exhibit a high degree of sequence homology to cathepsin B (EC 3.4.22.1) and other cysteine proteinases of the papain superfamily.
已测定人肾组织组织蛋白酶H(EC 3.4.22.16)和人肾组织组织蛋白酶L(EC 3.4.22.15)的完整氨基酸序列。组织蛋白酶H含有230个残基,相对分子质量为25116。该序列是通过对轻链、重链和小链以及该酶单链形式经溴化氰裂解产生的肽段进行测序获得的。糖基化的小链是组织蛋白酶H前肽的蛋白水解片段。人组织蛋白酶L有217个氨基酸残基,相对分子质量为23720。其氨基酸序列是根据重链和轻链的N端序列以及重链溴化氰片段的序列推导出来的。通过与来自其他物种的组织蛋白酶H和L的已知序列进行比较,将这些片段进行了比对。组织蛋白酶H和L与组织蛋白酶B(EC 3.4.22.1)以及木瓜蛋白酶超家族的其他半胱氨酸蛋白酶表现出高度的序列同源性。