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Partial characterization of a fraction from bull seminal vesicle fluid that potentiates the bull sperm acrosome reaction in vitro
Author(s) -
Rönkkö S.,
LinnalaKankkunen A.,
Tuhkanen A. L.
Publication year - 2009
Publication title -
andrologia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.633
H-Index - 59
eISSN - 1439-0272
pISSN - 0303-4569
DOI - 10.1111/j.1439-0272.1994.tb00760.x
Subject(s) - lysophosphatidylethanolamine , acrosome reaction , acrosome , chemistry , lysophosphatidylcholine , chromatography , vesicle , phosphatidylcholine , phospholipase a , sperm , size exclusion chromatography , biochemistry , seminal vesicle , phosphatidylethanolamine , phospholipase a2 , in vitro , phospholipid , enzyme , biology , membrane , prostate , botany , genetics , cancer
Summary. A fraction from bovine seminal vesicle fluid that initiated acrosome reaction of bovine epididymal spermatozoa in vitro in the presence of heparin was prepared by sequential chromatographies on heparin‐Sepharose, gel filtration (Superose 12) and reversed phase chromatography (ProRPC). Sequence analysis of the separated fraction showed that it contained the major protein (PDC‐109) with 100% homology. This fraction contained also Ca 2+ ‐dependent phospholipase A 2 ‐like activity which hydrolysed phosphatidylethanolamine and phosphatidylcholine with 14C‐labelled linoleic (lino‐PE, lino‐PC) or arachidonic acid (ara‐PE, ara‐PC) at sn‐2 position. This protein was not detected in N‐terminal sequence analysis. Lysophosphatidylcholine, lysophosphatidylethanolamine, and p‐bromophenacyl bromide (p‐BPB) inhibited this lipolytic activity. Sulfoglycolipid (Seminolipid) had inhibitory effect at concentrations above 0.1 mM but activated slightly the enzyme at lower concentrations. Boiling destroyed acrosome initiating activity in the separated fraction.