| Acid and neutral alpha-glucosidase in the reproductive organs and seminal plasma of the bull. | |
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MedLine Citation:
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PMID: 3900385 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A synthetic substrate (p-nitrophenyl-alpha-D-glucopyranoside) was used to measure the acid and neutral alpha-glucosidase activity in bull seminal plasma, spermatozoa and in homogenates of bull reproductive organs. Marked differences were observed in the activities of these enzymes in the various tissues studied. Epididymis and particularly its caput region contained the highest specific activity of acid alpha-glucosidase. The activity of neutral alpha-glucosidase was highest in testis and in different parts of the epididymis. Seminal plasma, spermatozoa and seminal vesicle secretion contained only the acid enzyme activity. After fractionation with anion exchange chromatography in HPLC (Mono Q) and chromatofocussing, acid alpha-glucosidase activity of seminal plasma was recovered in two fractions with different pI values. The corresponding activities were found in the secretion of seminal vesicles, which thus form the major secretory source of seminal plasma acid alpha-glucosidase. In the fractionation with gel filtration on Sepharose 6B, the acid alpha-glucosidase had a smaller molecular weight than did the neutral enzyme. In anion exchange chromatography and chromatofocussing the testicular and epididymal homogenates each contained two acid and two neutral isoenzymes. In both fractionations the elution pattern of acid alpha-glucosidase was clearly different from that of the enzymes in seminal plasma. The pH optimum of acid alpha-glucosidase ranged from 3.75 to 4.5 and that of the neutral enzyme from 6.5 to 7.0. The neutral activity was more sensitive to many divalent metal ions and differences were also observed in the response of the enzymes to different concentrations of turanose and KCl. |
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Authors:
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A Jauhiainen; T Vanha-Perttula |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of reproduction and fertility Volume: 74 ISSN: 0022-4251 ISO Abbreviation: J. Reprod. Fertil. Publication Date: 1985 Jul |
Date Detail:
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Created Date: 1985-10-31 Completed Date: 1985-10-31 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0376367 Medline TA: J Reprod Fertil Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 669-80 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Body Fluids / enzymology Cattle Chromatography, High Pressure Liquid Chromatography, Ion Exchange Epididymis / enzymology Genitalia, Male / enzymology* Glucosidases / analysis* Hot Temperature Hydrogen-Ion Concentration Male Semen / enzymology* Seminal Vesicles / secretion Spermatozoa / enzymology* alpha-Glucosidases / analysis* |
| Chemical | |
Reg. No./Substance:
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EC 3.2.1.-/Glucosidases; EC 3.2.1.20/alpha-Glucosidases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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