A microassay for the peptidase activity of enzymes utilizing ribonuclease S peptide as a substrate
A microassay for the peptidase activity of proteins obtained in minute amounts was devised. The method uses ribonuclease S peptide as a substrate. The substrate when cleaved is unable to reconstitute an active ribonuclease S complex. Therefore the loss in activity of the reconstituted complex is a m...
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Veröffentlicht in: | Analytical biochemistry 1978, Vol.84 (1), p.343-345 |
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container_title | Analytical biochemistry |
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creator | Levit, Shimon Joshi, Madhusudan S. |
description | A microassay for the peptidase activity of proteins obtained in minute amounts was devised. The method uses ribonuclease S peptide as a substrate. The substrate when cleaved is unable to reconstitute an active ribonuclease S complex. Therefore the loss in activity of the reconstituted complex is a measure of the peptidase activity. The method was previously tested with known peptidases such as clastase (9), chymotrypsin (8), and trypsin. In this work the peptidase activity of a protein related to a sperm-decapitating factor (1) is evidenced. |
doi_str_mv | 10.1016/0003-2697(78)90522-5 |
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The method uses ribonuclease S peptide as a substrate. The substrate when cleaved is unable to reconstitute an active ribonuclease S complex. Therefore the loss in activity of the reconstituted complex is a measure of the peptidase activity. The method was previously tested with known peptidases such as clastase (9), chymotrypsin (8), and trypsin. In this work the peptidase activity of a protein related to a sperm-decapitating factor (1) is evidenced.</description><identifier>ISSN: 0003-2697</identifier><identifier>EISSN: 1096-0309</identifier><identifier>DOI: 10.1016/0003-2697(78)90522-5</identifier><identifier>PMID: 580168</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Female ; Male ; Microchemistry ; Peptide Fragments - metabolism ; Peptide Hydrolases - metabolism ; Pregnancy ; Proestrus ; Rats ; Ribonucleases - metabolism ; Sperm Capacitation ; Uterus - enzymology</subject><ispartof>Analytical biochemistry, 1978, Vol.84 (1), p.343-345</ispartof><rights>1978</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-7f68421efac0d7c31f6b8ed9bba0e3203e6d6840e9886e3c12a1c2a9a67da7913</citedby><cites>FETCH-LOGICAL-c356t-7f68421efac0d7c31f6b8ed9bba0e3203e6d6840e9886e3c12a1c2a9a67da7913</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003269778905225$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,4009,27902,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/580168$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Levit, Shimon</creatorcontrib><creatorcontrib>Joshi, Madhusudan S.</creatorcontrib><title>A microassay for the peptidase activity of enzymes utilizing ribonuclease S peptide as a substrate</title><title>Analytical biochemistry</title><addtitle>Anal Biochem</addtitle><description>A microassay for the peptidase activity of proteins obtained in minute amounts was devised. The method uses ribonuclease S peptide as a substrate. The substrate when cleaved is unable to reconstitute an active ribonuclease S complex. Therefore the loss in activity of the reconstituted complex is a measure of the peptidase activity. The method was previously tested with known peptidases such as clastase (9), chymotrypsin (8), and trypsin. In this work the peptidase activity of a protein related to a sperm-decapitating factor (1) is evidenced.</description><subject>Animals</subject><subject>Female</subject><subject>Male</subject><subject>Microchemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Pregnancy</subject><subject>Proestrus</subject><subject>Rats</subject><subject>Ribonucleases - metabolism</subject><subject>Sperm Capacitation</subject><subject>Uterus - enzymology</subject><issn>0003-2697</issn><issn>1096-0309</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kDtPwzAUhS3EqxT-QQdPCIaAHSe2syBVFS-pEgMwW45zA0Z5FNuplP56ElIxMt3hfOdI90NoQckNJZTfEkJYFPNMXAl5nZE0jqP0AM0oyXhEGMkO0ewPOUVn3n8RQmmS8hN0nMphQc5QvsS1Na7V3usel63D4RPwBjbBFtoD1ibYrQ09bksMza6vweMu2MrubPOBnc3bpjMVjOjrvjaUPNbYd7kPTgc4R0elrjxc7O8cvT_cv62eovXL4_NquY4MS3mIRMllElMotSGFMIyWPJdQZHmuCbCYMODFQBDIpOTADI01NbHONBeFFhllc3Q57W5c-92BD6q23kBV6QbazivJJE8ETQcwmcDhb-8dlGrjbK1dryhRo1k1alOjNiWk-jWrxtpiv9_lNRR_pUnlEN9NMQw_bi045Y2FxkBhHZigitb-v_8DNCmJHA</recordid><startdate>1978</startdate><enddate>1978</enddate><creator>Levit, Shimon</creator><creator>Joshi, Madhusudan S.</creator><general>Elsevier Inc</general><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>1978</creationdate><title>A microassay for the peptidase activity of enzymes utilizing ribonuclease S peptide as a substrate</title><author>Levit, Shimon ; Joshi, Madhusudan S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-7f68421efac0d7c31f6b8ed9bba0e3203e6d6840e9886e3c12a1c2a9a67da7913</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Animals</topic><topic>Female</topic><topic>Male</topic><topic>Microchemistry</topic><topic>Peptide Fragments - metabolism</topic><topic>Peptide Hydrolases - metabolism</topic><topic>Pregnancy</topic><topic>Proestrus</topic><topic>Rats</topic><topic>Ribonucleases - metabolism</topic><topic>Sperm Capacitation</topic><topic>Uterus - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Levit, Shimon</creatorcontrib><creatorcontrib>Joshi, Madhusudan S.</creatorcontrib><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>Analytical biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Levit, Shimon</au><au>Joshi, Madhusudan S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A microassay for the peptidase activity of enzymes utilizing ribonuclease S peptide as a substrate</atitle><jtitle>Analytical biochemistry</jtitle><addtitle>Anal Biochem</addtitle><date>1978</date><risdate>1978</risdate><volume>84</volume><issue>1</issue><spage>343</spage><epage>345</epage><pages>343-345</pages><issn>0003-2697</issn><eissn>1096-0309</eissn><abstract>A microassay for the peptidase activity of proteins obtained in minute amounts was devised. The method uses ribonuclease S peptide as a substrate. The substrate when cleaved is unable to reconstitute an active ribonuclease S complex. Therefore the loss in activity of the reconstituted complex is a measure of the peptidase activity. The method was previously tested with known peptidases such as clastase (9), chymotrypsin (8), and trypsin. In this work the peptidase activity of a protein related to a sperm-decapitating factor (1) is evidenced.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>580168</pmid><doi>10.1016/0003-2697(78)90522-5</doi><tpages>3</tpages></addata></record> |
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source | MEDLINE; Elsevier ScienceDirect Journals |
subjects | Animals Female Male Microchemistry Peptide Fragments - metabolism Peptide Hydrolases - metabolism Pregnancy Proestrus Rats Ribonucleases - metabolism Sperm Capacitation Uterus - enzymology |
title | A microassay for the peptidase activity of enzymes utilizing ribonuclease S peptide as a substrate |
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