Literature DB >> 13635006

Structural correlation between esterase and protease activities on trypsin.

L AUGENSTINE.   

Abstract

It is tentatively concluded from ultraviolet and x-ray studies that the two tryptic activities are mediated by overlapping "enzymatic sites." Crucial to this conclusion were studies of the factors which can modify the measured inactivation rates. The data are interpreted in the light of postulated mechanisms of inactivation.

Keywords:  ESTERASES; PROTEASES; TRYPSIN

Mesh：

Substances：

Year:  1959        PMID： 13635006     DOI： 10.1126/science.129.3350.718

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  4 in total

1.  [EFFECT OF ACTINOMYCIN ON THE PROPAGATION OF MYXOVIRUSES].

Authors:  R ROTT; C SCHOLTISSEK
Journal:  Z Naturforsch B       Date:  1964-04       Impact factor: 1.047

2.  The inactivation of trypsin by ultraviolet light. I. The correlation of inactivation with the disruption of constituent cystine.

Authors:  L G AUGENSTINE; C A GHIRON
Journal:  Proc Natl Acad Sci U S A       Date:  1961-10-15       Impact factor: 11.205

3.  The inactivation of trypsin by ultraviolet light. II. The involvement of intramolecular hydrogen bond disruption.

Authors:  L G AUGENSTINE; C A GHIRON; K L GRIST; R MASON
Journal:  Proc Natl Acad Sci U S A       Date:  1961-11-15       Impact factor: 11.205

4.  A comparison of the effects of ultraviolet and ionizing radiations on trypsin activity and on its constituent amino acids.

Authors:  M Burke; L Augenstein
Journal:  Biochem J       Date:  1969-09       Impact factor: 3.857
  4 in total

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