Literature DB >> 4906908

Negative homotropic interactions in binding of substrate to alkaline phosphatase of Escherichia coli.

R T Simpson, B L Valee.   

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Year:  1970        PMID： 4906908     DOI： 10.1021/bi00806a035

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


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  3 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.  Role of magnesium in Escherichia coli alkaline phosphatase.

Authors:  R A Anderson; W F Bosron; F S Kennedy; B L Vallee
Journal:  Proc Natl Acad Sci U S A       Date:  1975-08       Impact factor: 11.205

3.  Mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis.

Authors:  E M Fielden; P B Roberts; R C Bray; D J Lowe; G N Mautner; G Rotilio; L Calabrese
Journal:  Biochem J       Date:  1974-04       Impact factor: 3.857
  3 in total

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