Literature DB >> 2751672

A unique proteolytic action of HCE, a constituent protease of a fish hatching enzyme: tight binding to its natural substrate, egg envelope.

S Yasumasu1, S Katow, Y Umino, I Iuchi, K Yamagami.   

Abstract

High choriolytic enzyme (HCE), a constituent protease of the hatching enzyme of the teleost, Oryzias latipes, swells its natural substrate, egg envelope (chorion) by hydrolyzing it partially. This enzyme was found to be bound tightly to the chorion when it exerted catalytic action. This was evidenced by the experimental results showing (i) that the turnover of this enzyme seemed to be hindered by the chorion, (ii) that the enzyme bound to the chorion could be recovered by washing with an alkaline medium, and (iii) that the bound enzyme could be quantified by radioimmunological estimation. The bound enzyme sustained its original activity and the binding between the enzyme and the chorion seems to be stoichiometric.

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Year:  1989        PMID: 2751672     DOI: 10.1016/0006-291x(89)91961-x

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


  4 in total

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Journal:  Proc Natl Acad Sci U S A       Date:  1996-05-14       Impact factor: 11.205

4.  Intron-loss evolution of hatching enzyme genes in Teleostei.

Authors:  Mari Kawaguchi; Junya Hiroi; Masaki Miya; Mutsumi Nishida; Ichiro Iuchi; Shigeki Yasumasu
Journal:  BMC Evol Biol       Date:  2010-08-27       Impact factor: 3.260

  4 in total

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