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 Polakoski, K. L. Articles by Parrish, R. F. Search for Related Content PubMed PubMed Citation Articles by Polakoski, K. L. Articles by Parrish, R. F. Social Bookmarking                      What's this?

JBC, Vol. 252, Issue 6, 1888-1894, Mar, 1977

Boar proacrosin. Purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm

K. L. Polakoski and R. F. Parrish

Two forms of proacrosin have been purified from ejacualted boar spermatozoa. The isolation method utilized benzamidine to inhibit the premeture activation of the zymogen and included pH precipitation, ammonium sulfate fractionation, and sodium chloride precipitation. Further purification was achieved by Sephadex G-200 FILTRATION OF THE PREPARATION AFTER IT WAS TREATED WITH 8 M urea. The overall proacrosin yield was 58% with a specific acitivity of 253 units/mg of protein. The molecular weights of the proacrosins determined by sodium dodecyl sulfate disc gel electrophoresis were 55,000 and 53,000. Proacrosin autoactivation followed the classical S-shaped activation curve and calcium was not required to obtain full activation. Time course activation studies in 0.1 M Tris/HCl, pH 8.4, at 0 degrees were monitored with sodium dodecyl sulfate-disc gel eletrophoresis and anlytical gel electrophoresis with staining techniques for protein and enzymatic activity. Under the conditions used, the zymogens were sequentially degraded to three different active specise of acrosin (alpha, beta, and gamma). The approximate molecualr weights of the acrosins were 49,000, 39,000, and 25,000 for the alpha, beta, and gamma forms, respectively. The autoactivation is concentration-dependent and can be proteolytically stimulated with either alpha- or beta-acrosin and trypsin, indicating the activation of proacrosin can via a bimolecular process.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				C. Dube, P. Leclerc, T. Baba, C. Reyes-Moreno, and J. L. Bailey The Proacrosin Binding Protein, sp32, Is Tyrosine Phosphorylated During Capacitation of Pig Sperm J Androl, July 1, 2005; 26(4): 519 - 528. [Abstract] [Full Text] [PDF]

				R.D. Moreno and C. Barros A Basic 18-Amino Acid Peptide Contains the Polysulfate-Binding Domain Responsible for Activation of the Boar Proacrosin/Acrosin System Biol Reprod, June 1, 2000; 62(6): 1536 - 1542. [Abstract] [Full Text]

				T. Wincek, R. Parrish, and K. Polakoski Fertilization: a uterine glycosaminoglycan stimulates the conversion of sperm proacrosin to acrosin Science, February 9, 1979; 203(4380): 553 - 554. [Abstract] [PDF]