Literature DB >> 5330067

Measurement of the zinc dissociation constants of alkaline phosphatase from Escherichia coli by equilibration with zinc ion buffers.

S R Cohen, I B Wilson.   

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Year:  1966        PMID： 5330067     DOI： 10.1021/bi00867a014

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  5 in total

1.  Studies on the active center of alkaline phosphatase of E. coli.

Authors:  G H Tait; B L Vallee
Journal:  Proc Natl Acad Sci U S A       Date:  1966-10       Impact factor: 11.205

2.  The binding of cupric ions to bovine pancreatic ribonuclease studies with diligand metal-ion buffers.

Authors:  R H Saundry; W D Stein
Journal:  Biochem J       Date:  1967-10       Impact factor: 3.857

3.  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

4.  The oxygen-linked zinc-binding site of human haemoglobin.

Authors:  J G Gilman; G J Brewer
Journal:  Biochem J       Date:  1978-03-01       Impact factor: 3.857

5.  Thionein/metallothionein control Zn(II) availability and the activity of enzymes.

Authors:  Artur Krezel; Wolfgang Maret
Journal:  J Biol Inorg Chem       Date:  2007-12-12       Impact factor: 3.358
  5 in total

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