Literature DB >> 4114668

Chemical modification of carboxypeptidase A crystals. Azo coupling with tyrosine-248.

J T Johansen, D M Livingston, B L Vallee.   

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Year:  1972        PMID： 4114668     DOI： 10.1021/bi00764a005

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


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  6 in total

1.  Resonance Raman spectroscopy of arsanilazocarboxypeptidase A: determination of the nature of the azotyrosyl-248-zinc complex.

Authors:  R K Scheule; H E Van Wart; B L Vallee; H A Scheraga
Journal:  Proc Natl Acad Sci U S A       Date:  1977-08       Impact factor: 11.205

2.  Similarities between the conformation of arsanilazotyrosine 248 of carboxypeptidase A in the crystalline state and in solution.

Authors:  F A Quiocho; C H McMurray; W N Lipscomb
Journal:  Proc Natl Acad Sci U S A       Date:  1972-10       Impact factor: 11.205

3.  Conformations of arsanilazotyrosine-248 carboxypeptidase A alpha, beta, gamma, comparison of crystals and solution.

Authors:  J T Johansen; B L Vallee
Journal:  Proc Natl Acad Sci U S A       Date:  1973-07       Impact factor: 11.205

4.  Carboxypeptidase A mechanisms.

Authors:  W N Lipscomb
Journal:  Proc Natl Acad Sci U S A       Date:  1980-07       Impact factor: 11.205

5.  Effects of pH on the structure and function of carboxypeptidase A: crystallographic studies.

Authors:  G Shoham; D C Rees; W N Lipscomb
Journal:  Proc Natl Acad Sci U S A       Date:  1984-12       Impact factor: 11.205

6.  Enzymatic activities of carobxypeptidase A's in solution and in crystals.

Authors:  W N Lipscomb
Journal:  Proc Natl Acad Sci U S A       Date:  1973-12       Impact factor: 11.205
  6 in total

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