Mammalian sperm acrosomal neuraminidases
A neuraminidase and a neuraminidase-like factor (NLF) were demonstrated for the first time in acrosomes of rabbit, bull, hamster, ram and human spermatozoa. The neuraminidase is similar to the known mammalian neuraminidases, but the NLF is unique in that it renders bound sialic acid reactive in Warr...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 1970-05, Vol.39 (4), p.575-582 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 582 |
|---|---|
| container_issue | 4 |
| container_start_page | 575 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 39 |
| creator | Srivastava, P.N. Zaneveld, L.J.D. Williams, William L. |
| description | A neuraminidase and a neuraminidase-like factor (NLF) were demonstrated for the first time in acrosomes of rabbit, bull, hamster, ram and human spermatozoa. The neuraminidase is similar to the known mammalian neuraminidases, but the NLF is unique in that it renders bound sialic acid reactive in Warren's colorimetric assay but does not release it from the macro-molecular complex. Partially purified decapacitation factor preparations that inhibit fertilization also inhibit NLF activity. The true neuraminidase activity appears to arise from NLF during purification. Cowpers gland mucin of the boar was used as substrate, and the effect of neuraminidase and NLF on this substrate was not duplicated by trypsin, α-chymotrypsin, pronase, α-amylase, lysozyme, hyaluronidase or detergents. |
| doi_str_mv | 10.1016/0006-291X(70)90242-1 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80745988</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0006291X70902421</els_id><sourcerecordid>80745988</sourcerecordid><originalsourceid>FETCH-LOGICAL-c381t-98e05e8f711551199a9d1cab34be124e764e68fd01fc58d9587bf7a8e499c6093</originalsourceid><addsrcrecordid>eNp9kE1Lw0AQhhdRaq3-A8WepB6iM5tNsnsRpPgFFQ9a8LZsNhNZyUfdbQT_vYktPXoamHlmmPdh7BThCgHTawBII67wfZbBpQIueIR7bIygIOIIYp-Nd8ghOwrhEwBRpGrERiLmKECN2ezZ1LWpnGmmYUW-nhrr29D2rWlDnTe1a1xhAoVjdlCaKtDJtk7Y8v7ubf4YLV4enua3i8jGEteRkgQJyTJDTBJEpYwq0Jo8FjkhF5SlglJZFoClTWShEpnlZWYkCaVsCiqesIvN3ZVvvzoKa127YKmqTENtF7SETCRKyh4UG3B4OHgq9cq72vgfjaAHQXpIr4f0OgP9J0hjv3a2vd_lNRW7pa2Rfn6-mZem1ebDu6CXrxww7t0pwSXviZsNQb2Gb0deB-uosVQ4T3ati9b9_8IvU0V8sA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>80745988</pqid></control><display><type>article</type><title>Mammalian sperm acrosomal neuraminidases</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Srivastava, P.N. ; Zaneveld, L.J.D. ; Williams, William L.</creator><creatorcontrib>Srivastava, P.N. ; Zaneveld, L.J.D. ; Williams, William L.</creatorcontrib><description>A neuraminidase and a neuraminidase-like factor (NLF) were demonstrated for the first time in acrosomes of rabbit, bull, hamster, ram and human spermatozoa. The neuraminidase is similar to the known mammalian neuraminidases, but the NLF is unique in that it renders bound sialic acid reactive in Warren's colorimetric assay but does not release it from the macro-molecular complex. Partially purified decapacitation factor preparations that inhibit fertilization also inhibit NLF activity. The true neuraminidase activity appears to arise from NLF during purification. Cowpers gland mucin of the boar was used as substrate, and the effect of neuraminidase and NLF on this substrate was not duplicated by trypsin, α-chymotrypsin, pronase, α-amylase, lysozyme, hyaluronidase or detergents.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(70)90242-1</identifier><identifier>PMID: 4321409</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amylases ; Animals ; Biological Sciences ; Bulbourethral Glands - enzymology ; Cattle ; Chymotrypsin ; Clostridium perfringens - enzymology ; Colorimetry ; Cricetinae ; Detergents ; Glycoproteins ; Hot Temperature ; Humans ; Hyaluronoglucosaminidase ; Hydrogen-Ion Concentration ; Kinetics ; Male ; Mucins ; Muramidase ; Neuraminic Acids ; Neuraminidase ; Peptide Hydrolases ; Protein Denaturation ; Proteins ; Rabbits ; Sheep ; Spermatozoa - enzymology ; Surface-Active Agents ; Swine ; Trypsin</subject><ispartof>Biochemical and biophysical research communications, 1970-05, Vol.39 (4), p.575-582</ispartof><rights>1970</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c381t-98e05e8f711551199a9d1cab34be124e764e68fd01fc58d9587bf7a8e499c6093</citedby><cites>FETCH-LOGICAL-c381t-98e05e8f711551199a9d1cab34be124e764e68fd01fc58d9587bf7a8e499c6093</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006291X70902421$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4321409$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Srivastava, P.N.</creatorcontrib><creatorcontrib>Zaneveld, L.J.D.</creatorcontrib><creatorcontrib>Williams, William L.</creatorcontrib><title>Mammalian sperm acrosomal neuraminidases</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>A neuraminidase and a neuraminidase-like factor (NLF) were demonstrated for the first time in acrosomes of rabbit, bull, hamster, ram and human spermatozoa. The neuraminidase is similar to the known mammalian neuraminidases, but the NLF is unique in that it renders bound sialic acid reactive in Warren's colorimetric assay but does not release it from the macro-molecular complex. Partially purified decapacitation factor preparations that inhibit fertilization also inhibit NLF activity. The true neuraminidase activity appears to arise from NLF during purification. Cowpers gland mucin of the boar was used as substrate, and the effect of neuraminidase and NLF on this substrate was not duplicated by trypsin, α-chymotrypsin, pronase, α-amylase, lysozyme, hyaluronidase or detergents.</description><subject>Amylases</subject><subject>Animals</subject><subject>Biological Sciences</subject><subject>Bulbourethral Glands - enzymology</subject><subject>Cattle</subject><subject>Chymotrypsin</subject><subject>Clostridium perfringens - enzymology</subject><subject>Colorimetry</subject><subject>Cricetinae</subject><subject>Detergents</subject><subject>Glycoproteins</subject><subject>Hot Temperature</subject><subject>Humans</subject><subject>Hyaluronoglucosaminidase</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Male</subject><subject>Mucins</subject><subject>Muramidase</subject><subject>Neuraminic Acids</subject><subject>Neuraminidase</subject><subject>Peptide Hydrolases</subject><subject>Protein Denaturation</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>Sheep</subject><subject>Spermatozoa - enzymology</subject><subject>Surface-Active Agents</subject><subject>Swine</subject><subject>Trypsin</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1970</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1Lw0AQhhdRaq3-A8WepB6iM5tNsnsRpPgFFQ9a8LZsNhNZyUfdbQT_vYktPXoamHlmmPdh7BThCgHTawBII67wfZbBpQIueIR7bIygIOIIYp-Nd8ghOwrhEwBRpGrERiLmKECN2ezZ1LWpnGmmYUW-nhrr29D2rWlDnTe1a1xhAoVjdlCaKtDJtk7Y8v7ubf4YLV4enua3i8jGEteRkgQJyTJDTBJEpYwq0Jo8FjkhF5SlglJZFoClTWShEpnlZWYkCaVsCiqesIvN3ZVvvzoKa127YKmqTENtF7SETCRKyh4UG3B4OHgq9cq72vgfjaAHQXpIr4f0OgP9J0hjv3a2vd_lNRW7pa2Rfn6-mZem1ebDu6CXrxww7t0pwSXviZsNQb2Gb0deB-uosVQ4T3ati9b9_8IvU0V8sA</recordid><startdate>19700522</startdate><enddate>19700522</enddate><creator>Srivastava, P.N.</creator><creator>Zaneveld, L.J.D.</creator><creator>Williams, William L.</creator><general>Elsevier Inc</general><scope>FBQ</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>19700522</creationdate><title>Mammalian sperm acrosomal neuraminidases</title><author>Srivastava, P.N. ; Zaneveld, L.J.D. ; Williams, William L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c381t-98e05e8f711551199a9d1cab34be124e764e68fd01fc58d9587bf7a8e499c6093</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1970</creationdate><topic>Amylases</topic><topic>Animals</topic><topic>Biological Sciences</topic><topic>Bulbourethral Glands - enzymology</topic><topic>Cattle</topic><topic>Chymotrypsin</topic><topic>Clostridium perfringens - enzymology</topic><topic>Colorimetry</topic><topic>Cricetinae</topic><topic>Detergents</topic><topic>Glycoproteins</topic><topic>Hot Temperature</topic><topic>Humans</topic><topic>Hyaluronoglucosaminidase</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Male</topic><topic>Mucins</topic><topic>Muramidase</topic><topic>Neuraminic Acids</topic><topic>Neuraminidase</topic><topic>Peptide Hydrolases</topic><topic>Protein Denaturation</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>Sheep</topic><topic>Spermatozoa - enzymology</topic><topic>Surface-Active Agents</topic><topic>Swine</topic><topic>Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Srivastava, P.N.</creatorcontrib><creatorcontrib>Zaneveld, L.J.D.</creatorcontrib><creatorcontrib>Williams, William L.</creatorcontrib><collection>AGRIS</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Srivastava, P.N.</au><au>Zaneveld, L.J.D.</au><au>Williams, William L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mammalian sperm acrosomal neuraminidases</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1970-05-22</date><risdate>1970</risdate><volume>39</volume><issue>4</issue><spage>575</spage><epage>582</epage><pages>575-582</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>A neuraminidase and a neuraminidase-like factor (NLF) were demonstrated for the first time in acrosomes of rabbit, bull, hamster, ram and human spermatozoa. The neuraminidase is similar to the known mammalian neuraminidases, but the NLF is unique in that it renders bound sialic acid reactive in Warren's colorimetric assay but does not release it from the macro-molecular complex. Partially purified decapacitation factor preparations that inhibit fertilization also inhibit NLF activity. The true neuraminidase activity appears to arise from NLF during purification. Cowpers gland mucin of the boar was used as substrate, and the effect of neuraminidase and NLF on this substrate was not duplicated by trypsin, α-chymotrypsin, pronase, α-amylase, lysozyme, hyaluronidase or detergents.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4321409</pmid><doi>10.1016/0006-291X(70)90242-1</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1970-05, Vol.39 (4), p.575-582 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80745988 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amylases Animals Biological Sciences Bulbourethral Glands - enzymology Cattle Chymotrypsin Clostridium perfringens - enzymology Colorimetry Cricetinae Detergents Glycoproteins Hot Temperature Humans Hyaluronoglucosaminidase Hydrogen-Ion Concentration Kinetics Male Mucins Muramidase Neuraminic Acids Neuraminidase Peptide Hydrolases Protein Denaturation Proteins Rabbits Sheep Spermatozoa - enzymology Surface-Active Agents Swine Trypsin |
| title | Mammalian sperm acrosomal neuraminidases |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-03T05%3A55%3A59IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Mammalian%20sperm%20acrosomal%20neuraminidases&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Srivastava,%20P.N.&rft.date=1970-05-22&rft.volume=39&rft.issue=4&rft.spage=575&rft.epage=582&rft.pages=575-582&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/0006-291X(70)90242-1&rft_dat=%3Cproquest_cross%3E80745988%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=80745988&rft_id=info:pmid/4321409&rft_els_id=0006291X70902421&rfr_iscdi=true |