{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T13:54:49Z","timestamp":1772805289359,"version":"3.50.1"},"reference-count":40,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2005,4,26]],"date-time":"2005-04-26T00:00:00Z","timestamp":1114473600000},"content-version":"vor","delay-in-days":4804,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Exp. Zool."],"published-print":{"date-parts":[[1992,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p><jats:italic>Marthasterias glacialis<\/jats:italic> sperm cells were treated with ionophore A23187, centrifuged, and the supernatants were assayed for esterase activity. With N\u2010benzoyl\u2010L\u2010arginine ethyl ester\u2010HCl (BAEE) as substrate, a net activity was determined which was not detectable when N\u2010acetyl\u2010L\u2010tyrosine ethyl ester (ATEE) was used. The BAEE trypsin\u2010like activity was inhibited by soybean trypsin inhibitor (SBTI), N\u2010\u03b1\u2010p\u2010tosyl\u2010L\u2010lysine chloromethyl ketone\u2010HCl (TLCK), and phenyl methyl sulfonyl fluoride (PMSF), but not by L\u20101\u2010tosylamido\u20102\u2010phenylethyl chloromethyl ketone (TPCK). The presence of proteolytic activity in acrosomal exudates was further demonstrated by gelatin\u2010sodium dodecyl sulfate\u2010polyacrylamide gel electrophoretic zymography (gelatin\u2010SDS\u2010PAGE). The presence of several bands of low proteolytic activity and of one band of high proteolytic activity, which also has the lower molecular weight, together with the fact that all are inhibited by benzamidine, suggests the existence of a trypsin\u2010like proteinase system. The effect of the acrosomal exudate on the oocyte jelly coat was investigated by SDS\u2010PAGE analysis. All jelly proteins appeared to be digested by the acrosomal enzymes. Furthermore, if SBTI is added shortly after insemination, the sperm fail to fertilize the oocytes. These results indicate that the starfish sperm acrosomal vesicle contains a trypsin\u2010like protease which may be involved in sperm penetration through the oocyte jelly coat.<\/jats:p>","DOI":"10.1002\/jez.1402610314","type":"journal-article","created":{"date-parts":[[2005,6,11]],"date-time":"2005-06-11T00:12:34Z","timestamp":1118448754000},"page":"349-354","source":"Crossref","is-referenced-by-count":11,"title":["Presence of a trypsin\u2010like protease in starfish sperm acrosome"],"prefix":"10.1002","volume":"261","author":[{"given":"M\u00e1rio","family":"Sousa","sequence":"first","affiliation":[]},{"given":"Pedro","family":"Moradas\u2010Ferreira","sequence":"additional","affiliation":[]},{"given":"Carlos","family":"Azevedo","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,4,26]]},"reference":[{"key":"e_1_2_1_2_1","first-page":"385","article-title":"Localization of acrosomal enzymes in Arthropoda, Echinodermata and Vertebrata","volume":"21","author":"Baccetti B.","year":"1989","journal-title":"J. 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