Enzyme-Substrate Reactions in Very High Magnetic Fields. II
We have examined the effect of conditioning the enzyme trypsin in solution at pH 8.2 in a large magnetic field before determining its reactivity towards a synthetic substrate N-benzoyl DL-arginine p-nitroanilide (BAPA). This “pretreatment” was allowed to proceed for as long as 3⅔ hr in a magnetic fi...
Gespeichert in:
| Veröffentlicht in: | Biophysical journal 1967-07, Vol.7 (4), p.319-327 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 327 |
|---|---|
| container_issue | 4 |
| container_start_page | 319 |
| container_title | Biophysical journal |
| container_volume | 7 |
| creator | Rabinovitch, B. Maling, J.E. Weissbluth, M. |
| description | We have examined the effect of conditioning the enzyme trypsin in solution at pH 8.2 in a large magnetic field before determining its reactivity towards a synthetic substrate
N-benzoyl DL-arginine
p-nitroanilide (BAPA). This “pretreatment” was allowed to proceed for as long as 3⅔ hr in a magnetic field of 208 kgauss at temperatures 26 and 36°C. No effect on reactivity was observed when such pretreated enzyme solutions were compared with identical but untreated enzyme solutions. A single such reaction, allowed to proceed directly in a magnetic field of 220 kgauss for 9
min, similarly showed no difference in rate from its control. |
| doi_str_mv | 10.1016/S0006-3495(67)86591-3 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1368063</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006349567865913</els_id><sourcerecordid>84540610</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4433-d8948c94772bfd70faef25fb6828a77b72fe404ac55072eabe06c53a36ffa4d3</originalsourceid><addsrcrecordid>eNqFkEtLAzEUhYMoWh8_QZiV6GL0ZvIsgiLio6AIKm5DJnNTI9MZTaZC_fVObSm6cnUX59xzDh8h-xSOKVB58gQAMmd8KA6lOtJSDGnO1siACl7kAFquk8HKskW2U3oDoIUAukk2JXCtFR2Q06vmazbB_Glapi7aDrNHtK4LbZOy0GQvGGfZbRi_Zvd23GAXXHYdsK7ScTYa7ZINb-uEe8u7Q56vr54vb_O7h5vR5cVd7jhnLK_0kGs35EoVpa8UeIu-EL6UutBWqVIVHjlw64QAVaAtEaQTzDLpveUV2yFni9j3aTnBymHTD63NewwTG2emtcH8VZrwasbtp6FMapCsDzhYBsT2Y4qpM5OQHNa1bbCdJqO54CAp9EaxMLrYphTRr0oomDl08wPdzIkaqcwPdDMv2P-9cPW1pNzr5wsde0qfAaNJLmDjsAoRXWeqNvzT8A2TWZGX</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>84540610</pqid></control><display><type>article</type><title>Enzyme-Substrate Reactions in Very High Magnetic Fields. II</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><source>Open Access: Cell Press Free Archives</source><source>PubMed Central</source><source>EZB Electronic Journals Library</source><creator>Rabinovitch, B. ; Maling, J.E. ; Weissbluth, M.</creator><creatorcontrib>Rabinovitch, B. ; Maling, J.E. ; Weissbluth, M.</creatorcontrib><description>We have examined the effect of conditioning the enzyme trypsin in solution at pH 8.2 in a large magnetic field before determining its reactivity towards a synthetic substrate
N-benzoyl DL-arginine
p-nitroanilide (BAPA). This “pretreatment” was allowed to proceed for as long as 3⅔ hr in a magnetic field of 208 kgauss at temperatures 26 and 36°C. No effect on reactivity was observed when such pretreated enzyme solutions were compared with identical but untreated enzyme solutions. A single such reaction, allowed to proceed directly in a magnetic field of 220 kgauss for 9
min, similarly showed no difference in rate from its control.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(67)86591-3</identifier><identifier>PMID: 6048871</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Anilides - metabolism ; Arginine - metabolism ; Benzoates - metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Magnetics ; Spectrophotometry ; Temperature ; Trypsin - metabolism</subject><ispartof>Biophysical journal, 1967-07, Vol.7 (4), p.319-327</ispartof><rights>1967 The Biophysical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4433-d8948c94772bfd70faef25fb6828a77b72fe404ac55072eabe06c53a36ffa4d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1368063/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-3495(67)86591-3$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,3550,27924,27925,45995,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6048871$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rabinovitch, B.</creatorcontrib><creatorcontrib>Maling, J.E.</creatorcontrib><creatorcontrib>Weissbluth, M.</creatorcontrib><title>Enzyme-Substrate Reactions in Very High Magnetic Fields. II</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>We have examined the effect of conditioning the enzyme trypsin in solution at pH 8.2 in a large magnetic field before determining its reactivity towards a synthetic substrate
N-benzoyl DL-arginine
p-nitroanilide (BAPA). This “pretreatment” was allowed to proceed for as long as 3⅔ hr in a magnetic field of 208 kgauss at temperatures 26 and 36°C. No effect on reactivity was observed when such pretreated enzyme solutions were compared with identical but untreated enzyme solutions. A single such reaction, allowed to proceed directly in a magnetic field of 220 kgauss for 9
min, similarly showed no difference in rate from its control.</description><subject>Anilides - metabolism</subject><subject>Arginine - metabolism</subject><subject>Benzoates - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Magnetics</subject><subject>Spectrophotometry</subject><subject>Temperature</subject><subject>Trypsin - metabolism</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1967</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLAzEUhYMoWh8_QZiV6GL0ZvIsgiLio6AIKm5DJnNTI9MZTaZC_fVObSm6cnUX59xzDh8h-xSOKVB58gQAMmd8KA6lOtJSDGnO1siACl7kAFquk8HKskW2U3oDoIUAukk2JXCtFR2Q06vmazbB_Glapi7aDrNHtK4LbZOy0GQvGGfZbRi_Zvd23GAXXHYdsK7ScTYa7ZINb-uEe8u7Q56vr54vb_O7h5vR5cVd7jhnLK_0kGs35EoVpa8UeIu-EL6UutBWqVIVHjlw64QAVaAtEaQTzDLpveUV2yFni9j3aTnBymHTD63NewwTG2emtcH8VZrwasbtp6FMapCsDzhYBsT2Y4qpM5OQHNa1bbCdJqO54CAp9EaxMLrYphTRr0oomDl08wPdzIkaqcwPdDMv2P-9cPW1pNzr5wsde0qfAaNJLmDjsAoRXWeqNvzT8A2TWZGX</recordid><startdate>19670701</startdate><enddate>19670701</enddate><creator>Rabinovitch, B.</creator><creator>Maling, J.E.</creator><creator>Weissbluth, M.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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><scope>5PM</scope></search><sort><creationdate>19670701</creationdate><title>Enzyme-Substrate Reactions in Very High Magnetic Fields. II</title><author>Rabinovitch, B. ; Maling, J.E. ; Weissbluth, M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4433-d8948c94772bfd70faef25fb6828a77b72fe404ac55072eabe06c53a36ffa4d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1967</creationdate><topic>Anilides - metabolism</topic><topic>Arginine - metabolism</topic><topic>Benzoates - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Magnetics</topic><topic>Spectrophotometry</topic><topic>Temperature</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rabinovitch, B.</creatorcontrib><creatorcontrib>Maling, J.E.</creatorcontrib><creatorcontrib>Weissbluth, M.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rabinovitch, B.</au><au>Maling, J.E.</au><au>Weissbluth, M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzyme-Substrate Reactions in Very High Magnetic Fields. II</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1967-07-01</date><risdate>1967</risdate><volume>7</volume><issue>4</issue><spage>319</spage><epage>327</epage><pages>319-327</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>We have examined the effect of conditioning the enzyme trypsin in solution at pH 8.2 in a large magnetic field before determining its reactivity towards a synthetic substrate
N-benzoyl DL-arginine
p-nitroanilide (BAPA). This “pretreatment” was allowed to proceed for as long as 3⅔ hr in a magnetic field of 208 kgauss at temperatures 26 and 36°C. No effect on reactivity was observed when such pretreated enzyme solutions were compared with identical but untreated enzyme solutions. A single such reaction, allowed to proceed directly in a magnetic field of 220 kgauss for 9
min, similarly showed no difference in rate from its control.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6048871</pmid><doi>10.1016/S0006-3495(67)86591-3</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-3495 |
| ispartof | Biophysical journal, 1967-07, Vol.7 (4), p.319-327 |
| issn | 0006-3495 1542-0086 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1368063 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Open Access: Cell Press Free Archives; PubMed Central; EZB Electronic Journals Library |
| subjects | Anilides - metabolism Arginine - metabolism Benzoates - metabolism Hydrogen-Ion Concentration Kinetics Magnetics Spectrophotometry Temperature Trypsin - metabolism |
| title | Enzyme-Substrate Reactions in Very High Magnetic Fields. II |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-01T08%3A23%3A31IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Enzyme-Substrate%20Reactions%20in%20Very%20High%20Magnetic%20Fields.%20II&rft.jtitle=Biophysical%20journal&rft.au=Rabinovitch,%20B.&rft.date=1967-07-01&rft.volume=7&rft.issue=4&rft.spage=319&rft.epage=327&rft.pages=319-327&rft.issn=0006-3495&rft.eissn=1542-0086&rft_id=info:doi/10.1016/S0006-3495(67)86591-3&rft_dat=%3Cproquest_pubme%3E84540610%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=84540610&rft_id=info:pmid/6048871&rft_els_id=S0006349567865913&rfr_iscdi=true |