Literature DB >> 4829403

Differences between the conformations of nitrotyrosyl-248 carboxypeptidase A in the crystalline state and in solution.

J F Riordan, G Muszynska.   

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Year:  1974        PMID： 4829403     DOI： 10.1016/0006-291x(74)90951-6

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


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  4 in total

1.  Intramolecular arsanilazotyrosine-248-Zn complex of carboxypeptidase A: a monitor of multiple conformational states in solution.

Authors:  L W Harrison; D S Auld; B L Vallee
Journal:  Proc Natl Acad Sci U S A       Date:  1975-11       Impact factor: 11.205

2.  Carboxypeptidase A mechanisms.

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

3.  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

4.  The physical state dependence of carboxypeptidase Aalpha and Agamma kinetics.

Authors:  C A Spilburg; J L Bethune; B L Vallee
Journal:  Proc Natl Acad Sci U S A       Date:  1974-10       Impact factor: 11.205
  4 in total

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