Literature DB >> 4981035

Zinc-dependent conformational stability in the alkaline phosphatase of Escherichia coli.

C N Trotman, C Greenwood.   

Abstract

Entities:  

Mesh:

Substances:

Year:  1969        PMID: 4981035      PMCID: PMC1185041          DOI: 10.1042/bj1140082pb

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


× No keyword cloud information.
  3 in total

1.  Alkaline phosphatase of Escherichia coli: a zinc metalloenzyme.

Authors:  D J PLOCKE; C LEVINTHAL; B L VALLEE
Journal:  Biochemistry       Date:  1962-05-25       Impact factor: 3.162

2.  Two differentiable classes of metal atoms in alkaline phosphatase of Escherichia coli.

Authors:  R T Simpson; B L Vallee
Journal:  Biochemistry       Date:  1968-12       Impact factor: 3.162

3.  Activation of a mutationally altered form of the Escherichia coli alkaline phosphatase by zinc.

Authors:  M J Schlesinger
Journal:  J Biol Chem       Date:  1966-07-10       Impact factor: 5.157

  3 in total
  1 in total

1.  Effects of zinc and other metal ions on the stability and activity of Escherichia coli alkaline phosphatase.

Authors:  C N Trotman; C Greenwood
Journal:  Biochem J       Date:  1971-08       Impact factor: 3.857

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.