Peroxidase activities in bull spermatozoa
The present study was carried out to determine the localization of peroxidase activity in bull spermatozoa. 3,3′‐Diaminobenzidine (DAB) was used as a substrate for revealing peroxidase activity, and light and electron microscopic analysis of the results obtained was performed. Peroxidase activity wa...
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| Veröffentlicht in: | Molecular reproduction and development 1994-02, Vol.37 (2), p.204-209 |
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| creator | Pavlova, S. K. Kanchev, L. N. Alexandrov, M. Ts |
| description | The present study was carried out to determine the localization of peroxidase activity in bull spermatozoa. 3,3′‐Diaminobenzidine (DAB) was used as a substrate for revealing peroxidase activity, and light and electron microscopic analysis of the results obtained was performed. Peroxidase activity was detected in the mitochondria of the middle piece and the outer acrosomal membrane. Catalase was excluded as an enzyme, catalyzing the detected peroxidase activity. Concerning the biochemical properties of bull sperm peroxidases, peroxidase activity was found to be manifested in a large pH range, 4–10.5. Bull sperm peroxidase activity appeared to be temperature sensitive and azide sensitive and could be readily inhibited by phenylhydrazine. Electrophoretic analysis of the proteins from bull sperm extracts separated in a Davis‐Ornstein system of 7% polyacrylamide gel, followed by the determination of peroxidase activity on the polyacrylamide gels, revealed that all 14 sperm protein fractions available on the gel possessed peroxidase when benzidine was used as a substrate. The possible reasons for the electrophoretic heterogeneity of bull sperm peroxidases are discussed. © 1994 Wiley‐Liss, Inc. |
| doi_str_mv | 10.1002/mrd.1080370211 |
| format | Article |
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K. ; Kanchev, L. N. ; Alexandrov, M. Ts</creator><creatorcontrib>Pavlova, S. K. ; Kanchev, L. N. ; Alexandrov, M. Ts</creatorcontrib><description>The present study was carried out to determine the localization of peroxidase activity in bull spermatozoa. 3,3′‐Diaminobenzidine (DAB) was used as a substrate for revealing peroxidase activity, and light and electron microscopic analysis of the results obtained was performed. Peroxidase activity was detected in the mitochondria of the middle piece and the outer acrosomal membrane. Catalase was excluded as an enzyme, catalyzing the detected peroxidase activity. Concerning the biochemical properties of bull sperm peroxidases, peroxidase activity was found to be manifested in a large pH range, 4–10.5. Bull sperm peroxidase activity appeared to be temperature sensitive and azide sensitive and could be readily inhibited by phenylhydrazine. Electrophoretic analysis of the proteins from bull sperm extracts separated in a Davis‐Ornstein system of 7% polyacrylamide gel, followed by the determination of peroxidase activity on the polyacrylamide gels, revealed that all 14 sperm protein fractions available on the gel possessed peroxidase when benzidine was used as a substrate. The possible reasons for the electrophoretic heterogeneity of bull sperm peroxidases are discussed. © 1994 Wiley‐Liss, Inc.</description><identifier>ISSN: 1040-452X</identifier><identifier>EISSN: 1098-2795</identifier><identifier>DOI: 10.1002/mrd.1080370211</identifier><identifier>PMID: 8179903</identifier><identifier>CODEN: MREDEE</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>3,3'-Diaminobenzidine ; Acrosome - enzymology ; actividad enzimatica ; activite enzymatique ; Animals ; Biological and medical sciences ; Bull spermatozoa ; bulls ; Cattle ; Electrophoresis, Polyacrylamide Gel ; enzymic activity ; espermatozoo ; Fundamental and applied biological sciences. Psychology ; Histocytochemistry ; Male ; Mammalian male genital system ; Microscopy, Electron ; Mitochondria ; Mitochondria - enzymology ; Morphology. Physiology ; Outer acrosomal membrane ; peroxidasas ; Peroxidase activity ; peroxidases ; Peroxidases - isolation & purification ; Peroxidases - metabolism ; peroxydase ; spermatozoa ; Spermatozoa - enzymology ; Spermatozoa - ultrastructure ; spermatozoide ; Substrate Specificity ; taureau ; toro ; Vertebrates: reproduction</subject><ispartof>Molecular reproduction and development, 1994-02, Vol.37 (2), p.204-209</ispartof><rights>Copyright © 1994 Wiley‐Liss, Inc.</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4301-70dc8df1df38dc09069d1f7848651365704d63a5a9ea80fa64f822709adc64e03</citedby><cites>FETCH-LOGICAL-c4301-70dc8df1df38dc09069d1f7848651365704d63a5a9ea80fa64f822709adc64e03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fmrd.1080370211$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fmrd.1080370211$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3954791$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8179903$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pavlova, S. K.</creatorcontrib><creatorcontrib>Kanchev, L. N.</creatorcontrib><creatorcontrib>Alexandrov, M. Ts</creatorcontrib><title>Peroxidase activities in bull spermatozoa</title><title>Molecular reproduction and development</title><addtitle>Mol. Reprod. Dev</addtitle><description>The present study was carried out to determine the localization of peroxidase activity in bull spermatozoa. 3,3′‐Diaminobenzidine (DAB) was used as a substrate for revealing peroxidase activity, and light and electron microscopic analysis of the results obtained was performed. Peroxidase activity was detected in the mitochondria of the middle piece and the outer acrosomal membrane. Catalase was excluded as an enzyme, catalyzing the detected peroxidase activity. Concerning the biochemical properties of bull sperm peroxidases, peroxidase activity was found to be manifested in a large pH range, 4–10.5. Bull sperm peroxidase activity appeared to be temperature sensitive and azide sensitive and could be readily inhibited by phenylhydrazine. Electrophoretic analysis of the proteins from bull sperm extracts separated in a Davis‐Ornstein system of 7% polyacrylamide gel, followed by the determination of peroxidase activity on the polyacrylamide gels, revealed that all 14 sperm protein fractions available on the gel possessed peroxidase when benzidine was used as a substrate. The possible reasons for the electrophoretic heterogeneity of bull sperm peroxidases are discussed. © 1994 Wiley‐Liss, Inc.</description><subject>3,3'-Diaminobenzidine</subject><subject>Acrosome - enzymology</subject><subject>actividad enzimatica</subject><subject>activite enzymatique</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Bull spermatozoa</subject><subject>bulls</subject><subject>Cattle</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>enzymic activity</subject><subject>espermatozoo</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Histocytochemistry</subject><subject>Male</subject><subject>Mammalian male genital system</subject><subject>Microscopy, Electron</subject><subject>Mitochondria</subject><subject>Mitochondria - enzymology</subject><subject>Morphology. Physiology</subject><subject>Outer acrosomal membrane</subject><subject>peroxidasas</subject><subject>Peroxidase activity</subject><subject>peroxidases</subject><subject>Peroxidases - isolation & purification</subject><subject>Peroxidases - metabolism</subject><subject>peroxydase</subject><subject>spermatozoa</subject><subject>Spermatozoa - enzymology</subject><subject>Spermatozoa - ultrastructure</subject><subject>spermatozoide</subject><subject>Substrate Specificity</subject><subject>taureau</subject><subject>toro</subject><subject>Vertebrates: reproduction</subject><issn>1040-452X</issn><issn>1098-2795</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1PGzEQxS0E4iPlyg2UA0LqYdPx2ru2jyihQAu0asvHzRr8gQy72WBvWuCv70YbBfXU04w0v_fm6RGyR2FEAfJPdbTdIoEJyCldI9sUlMxyoYr1xc4h40V-t0V2UnoEAKUkbJJNSYVSwLbJx-8uNi_BYnJDNG34Hdrg0jBMh_fzqhqmmYs1ts1bgx_Ihscqud3lHJDrzye_xmfZxbfT8_HxRWY4A5oJsEZaT61n0hpQUCpLvZBclgVlZSGA25JhgcqhBI8l9zLPBSi0puQO2IAc9b6z2DzPXWp1HZJxVYVT18yTFiWXQkjZgaMeNLFJKTqvZzHUGF81Bb3oRnfd6PduOsH-0nl-Xzu7wpdldPfD5R2TwcpHnJqQVhhTBRdqYaN67E-o3Ot_nurLH5N_ImS9NqTWvay0GJ90KZgo9O3Vqf4yubn9enk10arjD3reY6PxIXZxrn9SpQoA2gko-wuC3ZN9</recordid><startdate>199402</startdate><enddate>199402</enddate><creator>Pavlova, S. K.</creator><creator>Kanchev, L. N.</creator><creator>Alexandrov, M. Ts</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>199402</creationdate><title>Peroxidase activities in bull spermatozoa</title><author>Pavlova, S. K. ; Kanchev, L. N. ; Alexandrov, M. Ts</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4301-70dc8df1df38dc09069d1f7848651365704d63a5a9ea80fa64f822709adc64e03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>3,3'-Diaminobenzidine</topic><topic>Acrosome - enzymology</topic><topic>actividad enzimatica</topic><topic>activite enzymatique</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Bull spermatozoa</topic><topic>bulls</topic><topic>Cattle</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>enzymic activity</topic><topic>espermatozoo</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Histocytochemistry</topic><topic>Male</topic><topic>Mammalian male genital system</topic><topic>Microscopy, Electron</topic><topic>Mitochondria</topic><topic>Mitochondria - enzymology</topic><topic>Morphology. Physiology</topic><topic>Outer acrosomal membrane</topic><topic>peroxidasas</topic><topic>Peroxidase activity</topic><topic>peroxidases</topic><topic>Peroxidases - isolation & purification</topic><topic>Peroxidases - metabolism</topic><topic>peroxydase</topic><topic>spermatozoa</topic><topic>Spermatozoa - enzymology</topic><topic>Spermatozoa - ultrastructure</topic><topic>spermatozoide</topic><topic>Substrate Specificity</topic><topic>taureau</topic><topic>toro</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pavlova, S. K.</creatorcontrib><creatorcontrib>Kanchev, L. N.</creatorcontrib><creatorcontrib>Alexandrov, M. Ts</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular reproduction and development</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pavlova, S. K.</au><au>Kanchev, L. N.</au><au>Alexandrov, M. Ts</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peroxidase activities in bull spermatozoa</atitle><jtitle>Molecular reproduction and development</jtitle><addtitle>Mol. Reprod. Dev</addtitle><date>1994-02</date><risdate>1994</risdate><volume>37</volume><issue>2</issue><spage>204</spage><epage>209</epage><pages>204-209</pages><issn>1040-452X</issn><eissn>1098-2795</eissn><coden>MREDEE</coden><abstract>The present study was carried out to determine the localization of peroxidase activity in bull spermatozoa. 3,3′‐Diaminobenzidine (DAB) was used as a substrate for revealing peroxidase activity, and light and electron microscopic analysis of the results obtained was performed. Peroxidase activity was detected in the mitochondria of the middle piece and the outer acrosomal membrane. Catalase was excluded as an enzyme, catalyzing the detected peroxidase activity. Concerning the biochemical properties of bull sperm peroxidases, peroxidase activity was found to be manifested in a large pH range, 4–10.5. Bull sperm peroxidase activity appeared to be temperature sensitive and azide sensitive and could be readily inhibited by phenylhydrazine. Electrophoretic analysis of the proteins from bull sperm extracts separated in a Davis‐Ornstein system of 7% polyacrylamide gel, followed by the determination of peroxidase activity on the polyacrylamide gels, revealed that all 14 sperm protein fractions available on the gel possessed peroxidase when benzidine was used as a substrate. The possible reasons for the electrophoretic heterogeneity of bull sperm peroxidases are discussed. © 1994 Wiley‐Liss, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>8179903</pmid><doi>10.1002/mrd.1080370211</doi><tpages>6</tpages></addata></record> |
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| subjects | 3,3'-Diaminobenzidine Acrosome - enzymology actividad enzimatica activite enzymatique Animals Biological and medical sciences Bull spermatozoa bulls Cattle Electrophoresis, Polyacrylamide Gel enzymic activity espermatozoo Fundamental and applied biological sciences. Psychology Histocytochemistry Male Mammalian male genital system Microscopy, Electron Mitochondria Mitochondria - enzymology Morphology. Physiology Outer acrosomal membrane peroxidasas Peroxidase activity peroxidases Peroxidases - isolation & purification Peroxidases - metabolism peroxydase spermatozoa Spermatozoa - enzymology Spermatozoa - ultrastructure spermatozoide Substrate Specificity taureau toro Vertebrates: reproduction |
| title | Peroxidase activities in bull spermatozoa |
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