Dufour E, Obled A, Valin C, Béchet D, Ribadeau-Dumas B, Huet J C
INRA Theix, Ceyrat, France.
Biochemistry. 1987 Sep 8;26(18):5689-95. doi: 10.1021/bi00392a017.
Cathepsin L was purified from chicken liver lysosomes by a two-step procedure. Cathepsin L exhibited a single band of Mr 27,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions, presented a high affinity for the substrate Z-Phe-Arg-NMec, was very unstable at neutral pH, and was inhibited by Z-Phe-Phe-CHN2. The complete amino acid sequence of cathepsin L has been determined and consists of 215 residues. The sequence was deduced from analysis of peptides generated by enzymatic digestions and by chemical cleavage at methionyl bonds. Comparison of the amino acid sequence of cathepsin L with those of rat liver cathepsins B and H and papain demonstrates a striking homology among their primary structures.
通过两步法从鸡肝溶酶体中纯化出组织蛋白酶L。在还原条件下，经十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析，组织蛋白酶L呈现出一条分子量为27,000的条带；它对底物Z-苯丙氨酸-精氨酸-甲基香豆素酰胺表现出高亲和力，在中性pH条件下非常不稳定，并受到Z-苯丙氨酸-苯丙氨酸-重氮甲烷的抑制。已确定组织蛋白酶L的完整氨基酸序列，由215个残基组成。该序列是通过对酶消化产生的肽段以及甲硫氨酸键处的化学裂解产物进行分析推导得出的。将组织蛋白酶L的氨基酸序列与大鼠肝脏组织蛋白酶B和H以及木瓜蛋白酶的序列进行比较，结果显示它们的一级结构具有显著的同源性。
