Literature DB >> 1426648

Localization of a chymotrypsin-like protease to the perivitelline space of Xenopus laevis eggs.

L L Lindsay1, C A Larabell, J L Hedrick.   

Abstract

A chymotrypsin-like protease is released from Xenopus laevis eggs at activation and is involved in conversion of the vitelline envelope to the fertilization envelope. To localize this enzyme in unactivated and activated eggs, we used the synthetic peptide substrate succinylalanylalanylprolylphenylalanyl-4-methoxy-2-naphthylamide whose product can be visualized using transmission electron microscopy. Protease product was localized within the perivitelline space of unactivated eggs, appearing as strings of beads. No protease activity was detected in activated eggs, which is consistent with the observation that the protease is released from the egg at activation.

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Year:  1992        PMID: 1426648     DOI: 10.1016/0012-1606(92)90081-q

Source DB:  PubMed          Journal:  Dev Biol        ISSN: 0012-1606            Impact factor:   3.582


  4 in total

1.  Ovochymase, a Xenopus laevis egg extracellular protease, is translated as part of an unusual polyprotease.

Authors:  L L Lindsay; J C Yang; J L Hedrick
Journal:  Proc Natl Acad Sci U S A       Date:  1999-09-28       Impact factor: 11.205

2.  Post-fertilization changes in the zona pellucida glycoproteins of rat eggs.

Authors:  T Raz; E Skutelsky; R Shalgi
Journal:  Histochem Cell Biol       Date:  1996-10       Impact factor: 4.304

3.  Conservation of sequence and function in fertilization of the cortical granule serine protease in echinoderms.

Authors:  Nathalie Oulhen; Dongdong Xu; Gary M Wessel
Journal:  Biochem Biophys Res Commun       Date:  2014-05-27       Impact factor: 3.575

4.  Structural Mechanics of the Alpha-2-Macroglobulin Transformation.

Authors:  Yasuhiro Arimura; Hironori Funabiki
Journal:  J Mol Biol       Date:  2021-12-20       Impact factor: 5.469

  4 in total

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