| Literature DB >> 3972105 |
A Ritonja, T Popovic, V Turk, K Wiedenmann, W Machleidt.
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.Entities:
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Year: 1985 PMID: 3972105 DOI: 10.1016/0014-5793(85)81136-4
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124