Literature DB >> 4900985

On the mechanism of the Zn2+ and Co2+-alkaline phosphatase of E. coli. Number of sites and anticooperativity.

C Lazdunski, C Petitclerc, D Chappelet, M Lazdunski.   

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Year:  1969        PMID： 4900985     DOI： 10.1016/0006-291x(69)90954-1

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


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  5 in total

1.  Steady-state kinetic studies of the negative co-operativity and flip-flop mechanism for Escherichia coli alkaline phosphatase.

Authors:  R D Waight; P Leff; W G Bardsley
Journal:  Biochem J       Date:  1977-12-01       Impact factor: 3.857

2.  Purification and characterization of specific 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase from Escherichia coli B.

Authors:  P H Ray; C D Benedict
Journal:  J Bacteriol       Date:  1980-04       Impact factor: 3.490

3.  Purification and characterization of 3-deoxy-D-manno-octulosonate 8-phosphate synthetase from Escherichia coli.

Authors:  P H Ray
Journal:  J Bacteriol       Date:  1980-02       Impact factor: 3.490

4.  Characterization of phosphate binding by alkaline phosphatase in rat kidney brush border membrane.

Authors:  R Beliveau; M G Brunette; J Strevey
Journal:  Pflugers Arch       Date:  1983-08       Impact factor: 3.657

Review 5.  Arsenic binding to proteins.

Authors:  Shengwen Shen; Xing-Fang Li; William R Cullen; Michael Weinfeld; X Chris Le
Journal:  Chem Rev       Date:  2013-06-28       Impact factor: 60.622
  5 in total

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