Immobilized pronase
Pronase was successfully coupled to an arylamino derivative of porous glass. The immobilized enzyme retains considerable activity against large and small substrates: bovine serum albumin, 57%; benzoyl-L-arginine ethylester, 27%; L-leucine-p-nitroanilide, 67%. Studies of enzyme stability, pH behavior...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1971-07, Vol.44 (2), p.426-432 |
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| container_title | Biochemical and biophysical research communications |
| container_volume | 44 |
| creator | Royer, G.P. Green, G.M. |
| description | Pronase was successfully coupled to an arylamino derivative of porous glass. The immobilized enzyme retains considerable activity against large and small substrates: bovine serum albumin, 57%; benzoyl-L-arginine ethylester, 27%; L-leucine-p-nitroanilide, 67%. Studies of enzyme stability, pH behavior and temperature dependence are presented. |
| doi_str_mv | 10.1016/0006-291X(71)90618-8 |
| format | Article |
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The immobilized enzyme retains considerable activity against large and small substrates: bovine serum albumin, 57%; benzoyl-L-arginine ethylester, 27%; L-leucine-p-nitroanilide, 67%. Studies of enzyme stability, pH behavior and temperature dependence are presented.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(71)90618-8</identifier><identifier>PMID: 5168513</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Anilides ; Animals ; Arginine ; Azo Compounds ; Benzoates ; Cattle ; Chemical Phenomena ; Chemistry ; Drug Stability ; Esters ; Glass ; Hydrogen-Ion Concentration ; Kinetics ; Leucine ; Nitrobenzenes ; Peptide Hydrolases ; Pronase ; Serum Albumin, Bovine ; Spectrophotometry ; Streptomyces - enzymology ; Thermodynamics</subject><ispartof>Biochemical and biophysical research communications, 1971-07, Vol.44 (2), p.426-432</ispartof><rights>1971</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-42c15883e47f537a2a28abd7c36284031aeaf96889a9419dd24702f782b8e3543</citedby><cites>FETCH-LOGICAL-c357t-42c15883e47f537a2a28abd7c36284031aeaf96889a9419dd24702f782b8e3543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(71)90618-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5168513$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Royer, G.P.</creatorcontrib><creatorcontrib>Green, G.M.</creatorcontrib><title>Immobilized pronase</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Pronase was successfully coupled to an arylamino derivative of porous glass. The immobilized enzyme retains considerable activity against large and small substrates: bovine serum albumin, 57%; benzoyl-L-arginine ethylester, 27%; L-leucine-p-nitroanilide, 67%. Studies of enzyme stability, pH behavior and temperature dependence are presented.</description><subject>Anilides</subject><subject>Animals</subject><subject>Arginine</subject><subject>Azo Compounds</subject><subject>Benzoates</subject><subject>Cattle</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Drug Stability</subject><subject>Esters</subject><subject>Glass</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Leucine</subject><subject>Nitrobenzenes</subject><subject>Peptide Hydrolases</subject><subject>Pronase</subject><subject>Serum Albumin, Bovine</subject><subject>Spectrophotometry</subject><subject>Streptomyces - enzymology</subject><subject>Thermodynamics</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1971</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kDtLA0EQxxdRYoxWtgpWosXpzr63EST4CARsFOyWvd05WLnLxduLoJ_eiwkprab4v_gNIWdAb4CCuqWUqoJZeL_ScG2pAlOYPTIGamnBgIp9Mt5ZDslRzh-UAghlR2QkQRkJfExOZ03TlqlOPxgvll278BmPyUHl64wn2zshb48Pr9PnYv7yNJvez4vApe4LwQJIYzgKXUmuPfPM-DLqwBUzgnLw6CurjLHeCrAxMqEpq7RhpUEuBZ-Qy03vsPu5wty7JuWAde0X2K6yM8C05EIORrExhq7NucPKLbvU-O7bAXXrX7g1qFuDOg3u7xfODLHzbf-qbDDuQlv4Qb_b6DhAfiXsXA4JFwFj6jD0Lrbp_4FfpJxq-g</recordid><startdate>19710716</startdate><enddate>19710716</enddate><creator>Royer, G.P.</creator><creator>Green, G.M.</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>19710716</creationdate><title>Immobilized pronase</title><author>Royer, G.P. ; Green, G.M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-42c15883e47f537a2a28abd7c36284031aeaf96889a9419dd24702f782b8e3543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1971</creationdate><topic>Anilides</topic><topic>Animals</topic><topic>Arginine</topic><topic>Azo Compounds</topic><topic>Benzoates</topic><topic>Cattle</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Drug Stability</topic><topic>Esters</topic><topic>Glass</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Leucine</topic><topic>Nitrobenzenes</topic><topic>Peptide Hydrolases</topic><topic>Pronase</topic><topic>Serum Albumin, Bovine</topic><topic>Spectrophotometry</topic><topic>Streptomyces - enzymology</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Royer, G.P.</creatorcontrib><creatorcontrib>Green, G.M.</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Royer, G.P.</au><au>Green, G.M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immobilized pronase</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1971-07-16</date><risdate>1971</risdate><volume>44</volume><issue>2</issue><spage>426</spage><epage>432</epage><pages>426-432</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Pronase was successfully coupled to an arylamino derivative of porous glass. 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| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1971-07, Vol.44 (2), p.426-432 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_81275345 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Anilides Animals Arginine Azo Compounds Benzoates Cattle Chemical Phenomena Chemistry Drug Stability Esters Glass Hydrogen-Ion Concentration Kinetics Leucine Nitrobenzenes Peptide Hydrolases Pronase Serum Albumin, Bovine Spectrophotometry Streptomyces - enzymology Thermodynamics |
| title | Immobilized pronase |
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