Substrate specificity of elastolytic and nonelastolytic proteinases from Pseudomonas aeruginosa
The points of cleavage of oxidized insulin B chain by nonelastolytic alkaline proteinase and elastase from Pseudomonas aeruginosa were compared. The two enzymes showed different specificities. The alkaline proteinase mainly split on the carboxyl side of bonds containing asparagine, cysteic acid, gly...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1966-04, Vol.114 (1), p.158-165 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Morihara, Kazuyuki Tsuzuki, Hiroshige |
| description | The points of cleavage of oxidized insulin B chain by nonelastolytic alkaline proteinase and elastase from
Pseudomonas aeruginosa were compared. The two enzymes showed different specificities. The alkaline proteinase mainly split on the carboxyl side of bonds containing asparagine, cysteic acid, glycine, glutamic acid, tyrosine, arginine, and phenylalanine, whereas the elastase split the bonds containing carboxyl groups of histidine, alanine, tyrosine, leucine, glycine, phenylalanine, and lysine. The alkaline proteinases from different strains showed no differences in specificity. The correlation between elastolysis and substrate specificity is discussed. |
| doi_str_mv | 10.1016/0003-9861(66)90317-1 |
| format | Article |
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Pseudomonas aeruginosa were compared. The two enzymes showed different specificities. The alkaline proteinase mainly split on the carboxyl side of bonds containing asparagine, cysteic acid, glycine, glutamic acid, tyrosine, arginine, and phenylalanine, whereas the elastase split the bonds containing carboxyl groups of histidine, alanine, tyrosine, leucine, glycine, phenylalanine, and lysine. The alkaline proteinases from different strains showed no differences in specificity. The correlation between elastolysis and substrate specificity is discussed.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(66)90317-1</identifier><identifier>PMID: 4959349</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Arginine - metabolism ; Asparagine - metabolism ; Chromatography ; Glutamates - metabolism ; Glycine - metabolism ; Insulin - metabolism ; Lysine - metabolism ; Pancreatic Elastase - metabolism ; Peptide Hydrolases - metabolism ; Peptides - metabolism ; Phenylalanine - metabolism ; Pseudomonas aeruginosa - enzymology ; Sulfonic Acids - metabolism ; Tyrosine - metabolism</subject><ispartof>Archives of biochemistry and biophysics, 1966-04, Vol.114 (1), p.158-165</ispartof><rights>1966</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c423t-5d70cd9578f977909693829ff7c42d1679bd5ff57ff48b779e993a03d21262393</citedby><cites>FETCH-LOGICAL-c423t-5d70cd9578f977909693829ff7c42d1679bd5ff57ff48b779e993a03d21262393</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003986166903171$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4959349$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Morihara, Kazuyuki</creatorcontrib><creatorcontrib>Tsuzuki, Hiroshige</creatorcontrib><title>Substrate specificity of elastolytic and nonelastolytic proteinases from Pseudomonas aeruginosa</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The points of cleavage of oxidized insulin B chain by nonelastolytic alkaline proteinase and elastase from
Pseudomonas aeruginosa were compared. The two enzymes showed different specificities. The alkaline proteinase mainly split on the carboxyl side of bonds containing asparagine, cysteic acid, glycine, glutamic acid, tyrosine, arginine, and phenylalanine, whereas the elastase split the bonds containing carboxyl groups of histidine, alanine, tyrosine, leucine, glycine, phenylalanine, and lysine. The alkaline proteinases from different strains showed no differences in specificity. The correlation between elastolysis and substrate specificity is discussed.</description><subject>Arginine - metabolism</subject><subject>Asparagine - metabolism</subject><subject>Chromatography</subject><subject>Glutamates - metabolism</subject><subject>Glycine - metabolism</subject><subject>Insulin - metabolism</subject><subject>Lysine - metabolism</subject><subject>Pancreatic Elastase - metabolism</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Peptides - metabolism</subject><subject>Phenylalanine - metabolism</subject><subject>Pseudomonas aeruginosa - enzymology</subject><subject>Sulfonic Acids - metabolism</subject><subject>Tyrosine - metabolism</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1966</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLxDAUhYMo4zj6DxS6El1Uk6ZNm40ggy8YUFDXIZPcSKRtxiQV5t-bOsPgytWFc859fQidEnxFMGHXGGOa84aRC8YuOaakzskemhLMWY5pU-6j6S5yiI5C-MSYkJIVEzQpecVpyadIvA7LEL2MkIUVKGussnGdOZNBK0N07TpalcleZ73r_0or7yLYXgYImfGuy14CDNp1LkmZBD982N4FeYwOjGwDnGzrDL3f373NH_PF88PT_HaRq7KgMa90jZXmVd0YXtc8vcBpU3Bj6uRrwmq-1JUxVW1M2SxTAjinElNdkIIVlNMZOt_MTXd9DRCi6GxQ0LayBzcE0ZQFaxgeg-UmqLwLwYMRK2876deCYDFyFSM0MUITjIlfroKktrPt_GHZgd41bUEm_2bjQ3ry24IXQVnoFWjrQUWhnf1_wQ8AJ4iX</recordid><startdate>196604</startdate><enddate>196604</enddate><creator>Morihara, Kazuyuki</creator><creator>Tsuzuki, Hiroshige</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>196604</creationdate><title>Substrate specificity of elastolytic and nonelastolytic proteinases from Pseudomonas aeruginosa</title><author>Morihara, Kazuyuki ; Tsuzuki, Hiroshige</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c423t-5d70cd9578f977909693829ff7c42d1679bd5ff57ff48b779e993a03d21262393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1966</creationdate><topic>Arginine - metabolism</topic><topic>Asparagine - metabolism</topic><topic>Chromatography</topic><topic>Glutamates - metabolism</topic><topic>Glycine - metabolism</topic><topic>Insulin - metabolism</topic><topic>Lysine - metabolism</topic><topic>Pancreatic Elastase - metabolism</topic><topic>Peptide Hydrolases - metabolism</topic><topic>Peptides - metabolism</topic><topic>Phenylalanine - metabolism</topic><topic>Pseudomonas aeruginosa - enzymology</topic><topic>Sulfonic Acids - metabolism</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Morihara, Kazuyuki</creatorcontrib><creatorcontrib>Tsuzuki, Hiroshige</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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Morihara, Kazuyuki</au><au>Tsuzuki, Hiroshige</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Substrate specificity of elastolytic and nonelastolytic proteinases from Pseudomonas aeruginosa</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1966-04</date><risdate>1966</risdate><volume>114</volume><issue>1</issue><spage>158</spage><epage>165</epage><pages>158-165</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The points of cleavage of oxidized insulin B chain by nonelastolytic alkaline proteinase and elastase from
Pseudomonas aeruginosa were compared. The two enzymes showed different specificities. The alkaline proteinase mainly split on the carboxyl side of bonds containing asparagine, cysteic acid, glycine, glutamic acid, tyrosine, arginine, and phenylalanine, whereas the elastase split the bonds containing carboxyl groups of histidine, alanine, tyrosine, leucine, glycine, phenylalanine, and lysine. The alkaline proteinases from different strains showed no differences in specificity. The correlation between elastolysis and substrate specificity is discussed.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4959349</pmid><doi>10.1016/0003-9861(66)90317-1</doi><tpages>8</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 1966-04, Vol.114 (1), p.158-165 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Arginine - metabolism Asparagine - metabolism Chromatography Glutamates - metabolism Glycine - metabolism Insulin - metabolism Lysine - metabolism Pancreatic Elastase - metabolism Peptide Hydrolases - metabolism Peptides - metabolism Phenylalanine - metabolism Pseudomonas aeruginosa - enzymology Sulfonic Acids - metabolism Tyrosine - metabolism |
| title | Substrate specificity of elastolytic and nonelastolytic proteinases from Pseudomonas aeruginosa |
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