Literature DB >> 7037751

Molecular weight and amino acid composition of a thermostable lytic endopeptidase.

E O Turkington, N E Welker.   

Abstract

A thermostable lytic endopeptidase from Bacillus stearothermophilus 1503-4R was purified 14,500-fold, with a 34% recovery of lytic activity. The enzyme is a basic protein (pI, 9.7) with a molecular weight of 15,100 and is composed of approximately 129 amino acid residues.

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Year:  1982        PMID： 7037751      PMCID： PMC220133          DOI： 10.1128/jb.150.1.418-420.1982

Source DB:  PubMed          Journal:  J Bacteriol        ISSN： 0021-9193            Impact factor:   3.490


  5 in total

1.  The spectrophotometric determination of tyrosine and tryptophan in proteins.

Authors:  T W Goodwin; R A Morton
Journal:  Biochem J       Date:  1946       Impact factor: 3.857

2.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

3.  The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.

Authors:  K Weber; M Osborn
Journal:  J Biol Chem       Date:  1969-08-25       Impact factor: 5.157

4.  Structure of the cell wall of Bacillus stearothermophiluys: mode of action of a thermophilic bacteriophage lytic enzyme.

Authors:  N E Welker
Journal:  J Bacteriol       Date:  1971-09       Impact factor: 3.490

5.  Purification and properties of a thermophilic bacteriophage lytic enzyme.

Authors:  N E Welker
Journal:  J Virol       Date:  1967-06       Impact factor: 5.103
  5 in total

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