Literature DB >> 16744342

The stereochemical specificity of esterases: The affinity of liver esterases for optically active alcohols.

D R Murray1, C G King.   

Abstract

Entities:  

Year:  1930        PMID： 16744342      PMCID： PMC1254371          DOI： 10.1042/bj0240190

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


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  1 in total

1.  Molecular constitution and accessibility to enzymes: The effect of various substances on the velocity of hydrolysis by pancreatic lipase.

Authors:  D R Murray
Journal:  Biochem J       Date:  1929       Impact factor: 3.857
  1 in total
  3 in total

1.  Studies on ali-esterases. V. Substrate specificity of the esterases of some saprophytic Mycobacteria.

Authors:  D K MYERS; J W TOL; M H DE JONGE
Journal:  Biochem J       Date:  1957-02       Impact factor: 3.857

2.  The inhibition of esterases by excess substrate.

Authors:  D R Murray
Journal:  Biochem J       Date:  1930       Impact factor: 3.857

3.  Studies on the relationship between chemical constitution and physiological action: The inhibitory action of certain synthetic urethanes on the activity of liver esterase.

Authors:  E Stedman; E Stedman
Journal:  Biochem J       Date:  1931       Impact factor: 3.857
  3 in total

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