Determination of leucine aminopeptidase using phenylalanyl-3-thia-phenylalanine as substrate
The peptide mimetic l-phenylalanyl- l-3-thiaphenylalanine has been shown to facilitate a sensitive and simple determination of leucine aminopeptidase. A colorimetric assay, employing Ellman's reagent to detect the thiophenol released upon hydrolysis of the dipeptide, has been developed. Under t...
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| Veröffentlicht in: | Analytical biochemistry 1986-05, Vol.154 (2), p.552-558 |
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| container_end_page | 558 |
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| container_issue | 2 |
| container_start_page | 552 |
| container_title | Analytical biochemistry |
| container_volume | 154 |
| creator | Hwang, Se Young Kingsbury, William D. Hall, Norman M. Jakas, Dalia R. Dunn, George L. Gilvarg, Charles |
| description | The peptide mimetic
l-phenylalanyl-
l-3-thiaphenylalanine has been shown to facilitate a sensitive and simple determination of leucine aminopeptidase. A colorimetric assay, employing Ellman's reagent to detect the thiophenol released upon hydrolysis of the dipeptide, has been developed. Under the experimental conditions employed the substrate has a
K
m
of 0.054 m
m and a
k
cat of 5800 min
−1 and can distinguish sharply between leucine aminopeptidase and aminopeptidase M. |
| doi_str_mv | 10.1016/0003-2697(86)90028-X |
| format | Article |
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l-phenylalanyl-
l-3-thiaphenylalanine has been shown to facilitate a sensitive and simple determination of leucine aminopeptidase. A colorimetric assay, employing Ellman's reagent to detect the thiophenol released upon hydrolysis of the dipeptide, has been developed. Under the experimental conditions employed the substrate has a
K
m
of 0.054 m
m and a
k
cat of 5800 min
−1 and can distinguish sharply between leucine aminopeptidase and aminopeptidase M.</description><identifier>ISSN: 0003-2697</identifier><identifier>EISSN: 1096-0309</identifier><identifier>DOI: 10.1016/0003-2697(86)90028-X</identifier><identifier>PMID: 2873758</identifier><identifier>CODEN: ANBCA2</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>aminopeptidase ; aminopeptidase (cytosol) ; aminopeptidase discrimination ; Aminopeptidases - metabolism ; Analytical, structural and metabolic biochemistry ; Applied sciences ; Biological and medical sciences ; calorimetry ; CD13 Antigens ; Chromogenic Compounds - chemical synthesis ; Chromogenic Compounds - metabolism ; Dipeptides - chemical synthesis ; Dipeptides - metabolism ; Enzymes and enzyme inhibitors ; Exact sciences and technology ; Fundamental and applied biological sciences. Psychology ; Humans ; Hydrolases ; Hydrolysis ; Kinetics ; leucine aminopeptidase ; Leucyl Aminopeptidase - metabolism ; Other techniques and industries ; peptidase substrate ; phenylalanyl-3-thia-phenylalanine ; serum aminopeptidase ; serum assay ; Spectrophotometry</subject><ispartof>Analytical biochemistry, 1986-05, Vol.154 (2), p.552-558</ispartof><rights>1986</rights><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c446t-6cc7fc2b6294cd48ce2081b74c6f6b76b8189ccb3a825ef96db1388eb0d70de43</citedby><cites>FETCH-LOGICAL-c446t-6cc7fc2b6294cd48ce2081b74c6f6b76b8189ccb3a825ef96db1388eb0d70de43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-2697(86)90028-X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8109375$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8134468$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2873758$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hwang, Se Young</creatorcontrib><creatorcontrib>Kingsbury, William D.</creatorcontrib><creatorcontrib>Hall, Norman M.</creatorcontrib><creatorcontrib>Jakas, Dalia R.</creatorcontrib><creatorcontrib>Dunn, George L.</creatorcontrib><creatorcontrib>Gilvarg, Charles</creatorcontrib><title>Determination of leucine aminopeptidase using phenylalanyl-3-thia-phenylalanine as substrate</title><title>Analytical biochemistry</title><addtitle>Anal Biochem</addtitle><description>The peptide mimetic
l-phenylalanyl-
l-3-thiaphenylalanine has been shown to facilitate a sensitive and simple determination of leucine aminopeptidase. A colorimetric assay, employing Ellman's reagent to detect the thiophenol released upon hydrolysis of the dipeptide, has been developed. Under the experimental conditions employed the substrate has a
K
m
of 0.054 m
m and a
k
cat of 5800 min
−1 and can distinguish sharply between leucine aminopeptidase and aminopeptidase M.</description><subject>aminopeptidase</subject><subject>aminopeptidase (cytosol)</subject><subject>aminopeptidase discrimination</subject><subject>Aminopeptidases - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Applied sciences</subject><subject>Biological and medical sciences</subject><subject>calorimetry</subject><subject>CD13 Antigens</subject><subject>Chromogenic Compounds - chemical synthesis</subject><subject>Chromogenic Compounds - metabolism</subject><subject>Dipeptides - chemical synthesis</subject><subject>Dipeptides - metabolism</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Exact sciences and technology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Hydrolases</subject><subject>Hydrolysis</subject><subject>Kinetics</subject><subject>leucine aminopeptidase</subject><subject>Leucyl Aminopeptidase - metabolism</subject><subject>Other techniques and industries</subject><subject>peptidase substrate</subject><subject>phenylalanyl-3-thia-phenylalanine</subject><subject>serum aminopeptidase</subject><subject>serum assay</subject><subject>Spectrophotometry</subject><issn>0003-2697</issn><issn>1096-0309</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1rFTEUhoMo9Vr9BwqzkKKL6Mkkk4-NIFWrUHCj0IUQkswZG5k7MyaZQv-9ub2X6666SeCc5305PIQ8Z_CGAZNvAYDTVhr1SsvXBqDV9OoB2TAwkgIH85Bsjshj8iTnXwCMiU6ekJNWK646vSE_PmDBtI2TK3GemnloRlxDnLBxdTgvuJTYu4zNmuP0s1mucbod3ejqSzkt19HRv7O7WG7y6nNJruBT8mhwY8Znh_-UfP_08dv5Z3r59eLL-ftLGoSQhcoQ1BBaL1sjQi90wBY080oEOUivpNdMmxA8d7rtcDCy94xrjR56BT0KfkrO9r1Lmn-vmIvdxhxwrCfhvGarpOFci-6fIBNCQCdVBcUeDGnOOeFglxS3Lt1aBnZn3-7U2p1aq6W9s2-vauzFoX_1W-yPoYPuun952Lsc3DgkN4WYj5hmvAr5DwxMravYuz2G1e1NxGRziDgF7GPCUGw_x_vP_QM3Cq8O</recordid><startdate>19860501</startdate><enddate>19860501</enddate><creator>Hwang, Se Young</creator><creator>Kingsbury, William D.</creator><creator>Hall, Norman M.</creator><creator>Jakas, Dalia R.</creator><creator>Dunn, George L.</creator><creator>Gilvarg, Charles</creator><general>Elsevier Inc</general><general>Elsevier</general><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19860501</creationdate><title>Determination of leucine aminopeptidase using phenylalanyl-3-thia-phenylalanine as substrate</title><author>Hwang, Se Young ; Kingsbury, William D. ; Hall, Norman M. ; Jakas, Dalia R. ; Dunn, George L. ; Gilvarg, Charles</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c446t-6cc7fc2b6294cd48ce2081b74c6f6b76b8189ccb3a825ef96db1388eb0d70de43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>aminopeptidase</topic><topic>aminopeptidase (cytosol)</topic><topic>aminopeptidase discrimination</topic><topic>Aminopeptidases - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Applied sciences</topic><topic>Biological and medical sciences</topic><topic>calorimetry</topic><topic>CD13 Antigens</topic><topic>Chromogenic Compounds - chemical synthesis</topic><topic>Chromogenic Compounds - metabolism</topic><topic>Dipeptides - chemical synthesis</topic><topic>Dipeptides - metabolism</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Exact sciences and technology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Hydrolases</topic><topic>Hydrolysis</topic><topic>Kinetics</topic><topic>leucine aminopeptidase</topic><topic>Leucyl Aminopeptidase - metabolism</topic><topic>Other techniques and industries</topic><topic>peptidase substrate</topic><topic>phenylalanyl-3-thia-phenylalanine</topic><topic>serum aminopeptidase</topic><topic>serum assay</topic><topic>Spectrophotometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hwang, Se Young</creatorcontrib><creatorcontrib>Kingsbury, William D.</creatorcontrib><creatorcontrib>Hall, Norman M.</creatorcontrib><creatorcontrib>Jakas, Dalia R.</creatorcontrib><creatorcontrib>Dunn, George L.</creatorcontrib><creatorcontrib>Gilvarg, Charles</creatorcontrib><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Analytical biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hwang, Se Young</au><au>Kingsbury, William D.</au><au>Hall, Norman M.</au><au>Jakas, Dalia R.</au><au>Dunn, George L.</au><au>Gilvarg, Charles</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Determination of leucine aminopeptidase using phenylalanyl-3-thia-phenylalanine as substrate</atitle><jtitle>Analytical biochemistry</jtitle><addtitle>Anal Biochem</addtitle><date>1986-05-01</date><risdate>1986</risdate><volume>154</volume><issue>2</issue><spage>552</spage><epage>558</epage><pages>552-558</pages><issn>0003-2697</issn><eissn>1096-0309</eissn><coden>ANBCA2</coden><abstract>The peptide mimetic
l-phenylalanyl-
l-3-thiaphenylalanine has been shown to facilitate a sensitive and simple determination of leucine aminopeptidase. A colorimetric assay, employing Ellman's reagent to detect the thiophenol released upon hydrolysis of the dipeptide, has been developed. Under the experimental conditions employed the substrate has a
K
m
of 0.054 m
m and a
k
cat of 5800 min
−1 and can distinguish sharply between leucine aminopeptidase and aminopeptidase M.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2873758</pmid><doi>10.1016/0003-2697(86)90028-X</doi><tpages>7</tpages></addata></record> |
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| ispartof | Analytical biochemistry, 1986-05, Vol.154 (2), p.552-558 |
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| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | aminopeptidase aminopeptidase (cytosol) aminopeptidase discrimination Aminopeptidases - metabolism Analytical, structural and metabolic biochemistry Applied sciences Biological and medical sciences calorimetry CD13 Antigens Chromogenic Compounds - chemical synthesis Chromogenic Compounds - metabolism Dipeptides - chemical synthesis Dipeptides - metabolism Enzymes and enzyme inhibitors Exact sciences and technology Fundamental and applied biological sciences. Psychology Humans Hydrolases Hydrolysis Kinetics leucine aminopeptidase Leucyl Aminopeptidase - metabolism Other techniques and industries peptidase substrate phenylalanyl-3-thia-phenylalanine serum aminopeptidase serum assay Spectrophotometry |
| title | Determination of leucine aminopeptidase using phenylalanyl-3-thia-phenylalanine as substrate |
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