HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Weidman, P. J. Articles by Shapiro, B. M. Search for Related Content PubMed PubMed Citation Articles by Weidman, P. J. Articles by Shapiro, B. M. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 262, Issue 31, 15076-15084, Nov, 1987

Purification and characterization of proteoliaisin, a coordinating protein in fertilization envelope assembly

PJ Weidman, DC Teller and BM Shapiro
Department of Biochemistry, University of Washington, Seattle 98195.

We report the purification and characterization of proteoliaisin, a protein that participates in the assembly of the sea urchin fertilization envelope. Proteoliaisin was purified from egg cortical granule exudate to greater than 99% homogeneity using chromatography on DEAE-Sepharose and on phenyl-Sepharose. Native proteoliaisin is a highly asymmetric protein (f/fo = 2.0) composed of a single Mr approximately 230,000 peptide. Its asymmetry was demonstrated both by analytical ultracentrifugation and by nondenaturing polyacrylamide gel electrophoresis, a novel analysis that detects molecular asymmetry in heterogeneous protein mixtures. Proteoliaisin is enriched in six amino acids: aspartic acid/asparagine, glutamic acid/glutamine, glycine, and cysteine, which account for over 50% of its mass. Nearly all of the cysteine residues are disulfide bonded. The protein contains a small proportion of aromatic amino acids with phenylalanine greater than tyrosine greater than tryptophan. At neutral pH its absorbance maximum is at 274.5 nm, with an extinction coefficient of 0.43 ml mg-1 cm-1. Proteoliaisin forms a 1:1 Ca2+-stabilized complex with ovoperoxidase, another component of the fertilization envelope, with Kd = 1.1 X 10(-6) M. Proteoliaisin, a constituent of the specialized echinoderm extracellular matrix called the fertilization envelope, has certain structural similarities to mammalian extracellular matrix proteins.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				S. A. Haley and G. M. Wessel Regulated Proteolysis by Cortical Granule Serine Protease 1 at Fertilization Mol. Biol. Cell, May 1, 2004; 15(5): 2084 - 2092. [Abstract] [Full Text] [PDF]

				G. M. Wessel, S. Conner, M. Laidlaw, J. Harrison, and G. J. LaFleur Jr SFE1, a Constituent of the Fertilization Envelope in the Sea Urchin Is Made by Oocytes and Contains Low-Density Lipoprotein-Receptor-Like Repeats Biol Reprod, December 1, 2000; 63(6): 1706 - 1712. [Abstract] [Full Text]

				N. Mozingo, C. Somers, and D. Chandler Ultrastructure of the proteoliaisin-ovoperoxidase complex and its spatial organization within the Strongylocentrotus purpuratus fertilization envelope J. Cell Sci., January 10, 1994; 107(10): 2769 - 2777. [Abstract] [PDF]

				B. Shapiro The control of oxidant stress at fertilization Science, April 26, 1991; 252(5005): 533 - 536. [Abstract] [PDF]