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人肝脏组织中组织蛋白酶B的氨基酸序列。

Amino acid sequence of human liver cathepsin B.

作者信息

Ritonja A, Popovic T, Turk V, Wiedenmann K, Machleidt W

出版信息

FEBS Lett. 1985 Feb 11;181(1):169-72. doi: 10.1016/0014-5793(85)81136-4.

Abstract

The complete amino acid sequence of cathepsin B (EC 3.4.22.1) from human liver was determined. The 252-residue sequence was obtained by automated solid-phase Edman degradation of the light and heavy chain resulting from limited proteolysis of the single-chain enzyme and of fragments produced by cyanogen bromide and enzymatic cleavage of the heavy chain. Human liver cathepsin B has 83.7% identical residues with the corresponding enzyme from rat liver. Comparison of both mammalian cathepsin B sequences with the sequence of papain provides further evidence that lysosomal and plant cysteine proteinases have evolved from a common ancestor and share a similar catalytic mechanism.

摘要

测定了人肝脏组织中组织蛋白酶B(EC 3.4.22.1)的完整氨基酸序列。通过对单链酶进行有限蛋白酶解产生的轻链和重链,以及通过溴化氰对重链进行酶解产生的片段进行自动固相埃德曼降解,获得了包含252个氨基酸残基的序列。人肝脏组织蛋白酶B与大鼠肝脏中的相应酶有83.7%的相同残基。将这两种哺乳动物组织蛋白酶B的序列与木瓜蛋白酶的序列进行比较,进一步证明了溶酶体和植物半胱氨酸蛋白酶是由一个共同的祖先进化而来的,并且具有相似的催化机制。

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