Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.27 (thermolysin)
 1,894 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An inactive form of acrosin was extracted from epididymal boar spermatozoa utilizing acid pH conditions. When subjected to activation in alkaline environment, this form turns into an enzymatically active species, which exhibits close-related electrophoretic characteristics. Both the precursor and the activated species, when incubated in the presence of thermolysin, give rise to two fastly moving acrosin molecular forms. In order to establish the nature of the true acrosin zymogen, we isolated poly(A+)-RNA from boar testicles, performed its translation in vitro in the presence of [35S]-methionine and reticulocyte lysate, immunoprecipitated the translation products with anti-boar acrosin antibody, and analyzed them by SDS-polyacrylamide gel electrophoresis and autoradiography. A single translation product of molecular weight 55,000 was detected. It is concluded that the polypeptide chain of the boar zymogen is of 55,000; increases in molecular weight are due to post-translational modifications, like glycosylation.
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PMID:Biochemical studies on proacrosin and acrosin from epididymal boar spermatozoa: in vitro translation of boar testicular proacrosin mRNA. 309 Oct 10

Acrosomal extracts of freshly ejaculated and immediately processed boar spermatozoa were investigated to detect which and how many acrosin molecular forms were present. Electrophoretic analyses of the acrosomal extract showed the presence of only one, slowly migrating, acrosin molecular form. Enzyme-linked-immuno-electro-transfer blot revealed the molecular weight of this form to be about 66 kdalton. Preliminary electrophoretic analyses under nondenaturating conditions of the acrosomal extract previously treated with thermolysin suggested that the approximately 66 kdalton form gives rise to two comigrating acrosin molecular forms.
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PMID:Evidence of a high molecular weight form of acrosin in boar acrosomal extract. 388 18