Multiple forms of carboxylesterase activity in Acinetobacter calcoaceticus
A carboxylesterase activity (E.C.3.1.1.) was found in all four strains of Acinetobacter calcoaceticus tested. The activity was present in both 2 × 104gav h−1 supernatant and bacterial wall‐membrane fractions. The activity in the supernatant was in two molecular weight forms, the predominant form wit...
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| Veröffentlicht in: | FEMS microbiology letters 1989-03, Vol.58 (1), p.75-79 |
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| creator | Sherwani, M.K. Fixter, L.M. |
| description | A carboxylesterase activity (E.C.3.1.1.) was found in all four strains of Acinetobacter calcoaceticus tested. The activity was present in both 2 × 104gav h−1 supernatant and bacterial wall‐membrane fractions. The activity in the supernatant was in two molecular weight forms, the predominant form with a Mr of about 103 K and a minor form Mr approximately 600 K. The activity was inhibited by phenylmethylsulfonyl fluoride. SDS‐PAGE showed that in A. calcoaceticus NCIB 8250 the activity was composed of three components of Mr 43, 40 and 38 K. The individual components showed different activities with 1‐ or 2‐naphthyl esters. Of the other strain used, one showed a nearly identical pattern of component activities, while the other two showed only two component activities. |
| doi_str_mv | 10.1111/j.1574-6968.1989.tb03021.x |
| format | Article |
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The activity was present in both 2 × 104gav h−1 supernatant and bacterial wall‐membrane fractions. The activity in the supernatant was in two molecular weight forms, the predominant form with a Mr of about 103 K and a minor form Mr approximately 600 K. The activity was inhibited by phenylmethylsulfonyl fluoride. SDS‐PAGE showed that in A. calcoaceticus NCIB 8250 the activity was composed of three components of Mr 43, 40 and 38 K. The individual components showed different activities with 1‐ or 2‐naphthyl esters. Of the other strain used, one showed a nearly identical pattern of component activities, while the other two showed only two component activities.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.1989.tb03021.x</identifier><identifier>PMID: 2721925</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Acinetobacter ; Acinetobacter - enzymology ; Bacteriology ; Biological and medical sciences ; Carboxylesterase ; Carboxylic Ester Hydrolases - analysis ; Fundamental and applied biological sciences. Psychology ; Metabolism. 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The activity was present in both 2 × 104gav h−1 supernatant and bacterial wall‐membrane fractions. The activity in the supernatant was in two molecular weight forms, the predominant form with a Mr of about 103 K and a minor form Mr approximately 600 K. The activity was inhibited by phenylmethylsulfonyl fluoride. SDS‐PAGE showed that in A. calcoaceticus NCIB 8250 the activity was composed of three components of Mr 43, 40 and 38 K. The individual components showed different activities with 1‐ or 2‐naphthyl esters. Of the other strain used, one showed a nearly identical pattern of component activities, while the other two showed only two component activities.</description><subject>Acinetobacter</subject><subject>Acinetobacter - enzymology</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Carboxylesterase</subject><subject>Carboxylic Ester Hydrolases - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>Molecular Weight</subject><subject>Multiple forms</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkF1r2zAUhsXY6NJsP2FgxtidPUm2vgq9CKHpWhJ6010LST4CBSfOJLtN_v0UYnI_3RzQ-5wPHoS-E1yR_H5tK8JEU3LFZUWUVNVgcY0pqY4f0OwafUQzXAtZEqzEZ3Sb0hZj3FDMb9ANFZQoymboeTN2Qzh0UPg-7lLR-8KZaPvjqYM0QDQJCuOG8BaGUxH2xcKFPQy9zX8QM9q53jgYghvTF_TJmy7B16nO0Z_Vw-vyd7l-eXxaLtalq5VgJWuVpZQIU9tWkcZwKagFbgFaaB32oDwWnjZM-YYSJ4zhyqmW2ppRi6Wt5-jnZe4h9n_HfKXeheSg68we-jFpwqisZUMyeHcBXexTiuD1IYadiSdNsD6L1Ft9tqXPtvRZpJ5E6mNu_jZtGe0O2mvrZC7nP6bcpKzBR7N3IV0xziTlkmfs_oK9hw5O_3GAXm3WgtX_ACwIkUA</recordid><startdate>198903</startdate><enddate>198903</enddate><creator>Sherwani, M.K.</creator><creator>Fixter, L.M.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</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></search><sort><creationdate>198903</creationdate><title>Multiple forms of carboxylesterase activity in Acinetobacter calcoaceticus</title><author>Sherwani, M.K. ; Fixter, L.M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3975-5d9b2217a3bd914a6872be6beededc0fe9f07f2459f421c7aa69c9d2b352b08b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Acinetobacter</topic><topic>Acinetobacter - enzymology</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Carboxylesterase</topic><topic>Carboxylic Ester Hydrolases - analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Metabolism. Enzymes</topic><topic>Microbiology</topic><topic>Molecular Weight</topic><topic>Multiple forms</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sherwani, M.K.</creatorcontrib><creatorcontrib>Fixter, L.M.</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><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sherwani, M.K.</au><au>Fixter, L.M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Multiple forms of carboxylesterase activity in Acinetobacter calcoaceticus</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>1989-03</date><risdate>1989</risdate><volume>58</volume><issue>1</issue><spage>75</spage><epage>79</epage><pages>75-79</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>A carboxylesterase activity (E.C.3.1.1.) was found in all four strains of Acinetobacter calcoaceticus tested. The activity was present in both 2 × 104gav h−1 supernatant and bacterial wall‐membrane fractions. The activity in the supernatant was in two molecular weight forms, the predominant form with a Mr of about 103 K and a minor form Mr approximately 600 K. The activity was inhibited by phenylmethylsulfonyl fluoride. SDS‐PAGE showed that in A. calcoaceticus NCIB 8250 the activity was composed of three components of Mr 43, 40 and 38 K. The individual components showed different activities with 1‐ or 2‐naphthyl esters. Of the other strain used, one showed a nearly identical pattern of component activities, while the other two showed only two component activities.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>2721925</pmid><doi>10.1111/j.1574-6968.1989.tb03021.x</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 1989-03, Vol.58 (1), p.75-79 |
| issn | 0378-1097 1574-6968 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_15283841 |
| source | Oxford University Press Journals Digital Archive legacy; MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Acinetobacter Acinetobacter - enzymology Bacteriology Biological and medical sciences Carboxylesterase Carboxylic Ester Hydrolases - analysis Fundamental and applied biological sciences. Psychology Metabolism. Enzymes Microbiology Molecular Weight Multiple forms |
| title | Multiple forms of carboxylesterase activity in Acinetobacter calcoaceticus |
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