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Amino acid sequence of human liver cathepsin B.
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.
PMID: 3972105 [PubMed - indexed for MEDLINE]
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Cited by 10 PubMed Central articles
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Extracellular-matrix degradation at acid pH. Avian osteoclast acid collagenase isolation and characterization.
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[Biochem J. 1993]
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Demonstration by electrospray mass spectrometry that the peptidyldipeptidase activity of cathepsin B is capable of rat cathepsin B C-terminal processing.
Rowan AD, Feng R, Konishi Y, Mort JS.
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[Biochem J. 1993]
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Rich DH, Brown MA, Barrett AJ.
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[Biochem J. 1986]
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