Literature DB >> 6391922

Primary structure of alpha-clostripain light chain.

A M Gilles, A Lecroisey, B Keil.   

Abstract

The primary structure of light chain of alpha-clostripain was determined by sequence analysis of peptides derived from tryptic digests purified by reverse-phase high-performance liquid chromatography. The 22 isolated tryptic peptides were aligned by peptides derived from chymotryptic and staphylococcal V8 proteinase digests. The light chain contains 133 amino acids residues and has a relative molecular mass of 15400. The prediction of its secondary structure is given.

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Year:  1984        PMID： 6391922     DOI： 10.1111/j.1432-1033.1984.tb08579.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN： 0014-2956


  4 in total

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Authors:  W J Neubert; C Eckerskorn; H E Homann
Journal:  Virus Genes       Date:  1991-01       Impact factor: 2.332

2.  Reverse action of hydrolases in frozen aqueous solutions.

Authors:  M Hänsler; H D Jakubke
Journal:  Amino Acids       Date:  1996-09       Impact factor: 3.520

3.  The heterodimeric protease clostripain from Clostridium histolyticum is encoded by a single gene.

Authors:  H Dargatz; T Diefenthal; V Witte; G Reipen; D von Wettstein
Journal:  Mol Gen Genet       Date:  1993-07

4.  The cysteine protease α-clostripain is not essential for the pathogenesis of Clostridium perfringens-mediated myonecrosis.

Authors:  Anjana Chakravorty; Milena M Awad; Thomas J Hiscox; Jackie K Cheung; Glen P Carter; Jocelyn M Choo; Dena Lyras; Julian I Rood
Journal:  PLoS One       Date:  2011-07-29       Impact factor: 3.240
  4 in total

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