Literature DB >> 6568226

Ovalbumin is an elastase substrate.

H T Wright.   

Abstract

Ovalbumin is partially homologous in sequence with the proteinase inhibitors alpha 1-proteinase inhibitor and anti-thrombin III. The region of sequence in ovalbumin which corresponds to the reactive sites of these proteinase inhibitors is susceptible to attack by subtilisin, elastase, thermolysin, bromelain, and Bacillus cereus protease. The esterase activity of elastase is not inhibited by ovalbumin, but ovalbumin is efficiently cleaved by elastase. In contrast with these proteases, trypsin does not cleave ovalbumin.

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Year:  1984        PMID: 6568226

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  4 in total

1.  Probing the serpin structural-transition mechanism in ovalbumin mutant R339T by proteolytic-cleavage kinetics of the reactive-centre loop.

Authors:  Yasuhiro Arii; Masaaki Hirose
Journal:  Biochem J       Date:  2002-04-15       Impact factor: 3.857

2.  Production and purification of Japanese quail ovalbumin as fusion protein with glutathione S-transferase in Escherichia coli.

Authors:  J Visvaderová; S Albert; A Kosová; J Klaudiny; J Simúth
Journal:  Folia Microbiol (Praha)       Date:  1995       Impact factor: 2.099

3.  Ovalbumin and angiotensinogen lack serpin S-R conformational change.

Authors:  P E Stein; D A Tewkesbury; R W Carrell
Journal:  Biochem J       Date:  1989-08-15       Impact factor: 3.857

4.  Evaluation of colorimetric assays for analyzing reductively methylated proteins: Biases and mechanistic insights.

Authors:  Pamlea N Brady; Megan A Macnaughtan
Journal:  Anal Biochem       Date:  2015-09-03       Impact factor: 3.365

  4 in total

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