Enzyme crypticity as an indicator of membrane orientation in envelope vesicles from halobacteria
A membrane fraction prepared by freeze-thawing envelope vesicles from Halobacterium halobium exhibits menadione-dependent NADH dehydrogenase activity (EC 1.6.9.9.3). The activity is “unmasked” by Triton X-100. Activity in freeze-thawed membrane preparations is more firmly membrane-bound than in soni...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1980-12, Vol.97 (4), p.1467-1473 |
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| container_title | Biochemical and biophysical research communications |
| container_volume | 97 |
| creator | Clark, Robert D. MacDonald, Russell E. |
| description | A membrane fraction prepared by freeze-thawing envelope vesicles from
Halobacterium halobium exhibits menadione-dependent NADH dehydrogenase activity (EC 1.6.9.9.3). The activity is “unmasked” by Triton X-100. Activity in freeze-thawed membrane preparations is more firmly membrane-bound than in sonicated vesicle preparations. Affinity for NADH is higher than in untreated vesicles and pyridine adenine dinucleotide specificity is the same. The data indicate that freeze-thawing causes reintegration of an adsorbed, extrinsic form of the dehydrogenase to yield an intrinsic, more native-like form of the enzyme. It is concluded that the extrinsic NADH dehydrogenase activity in vesicle preparations is not directly related to vesicle orientation. |
| doi_str_mv | 10.1016/S0006-291X(80)80030-1 |
| format | Article |
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Halobacterium halobium exhibits menadione-dependent NADH dehydrogenase activity (EC 1.6.9.9.3). The activity is “unmasked” by Triton X-100. Activity in freeze-thawed membrane preparations is more firmly membrane-bound than in sonicated vesicle preparations. Affinity for NADH is higher than in untreated vesicles and pyridine adenine dinucleotide specificity is the same. The data indicate that freeze-thawing causes reintegration of an adsorbed, extrinsic form of the dehydrogenase to yield an intrinsic, more native-like form of the enzyme. It is concluded that the extrinsic NADH dehydrogenase activity in vesicle preparations is not directly related to vesicle orientation.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(80)80030-1</identifier><identifier>PMID: 7213371</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Cell Membrane - enzymology ; Cell Membrane - ultrastructure ; Freezing ; Halobacterium - enzymology ; Halobacterium - ultrastructure ; NADH, NADPH Oxidoreductases - analysis ; Octoxynol ; Polyethylene Glycols ; Quinone Reductases - analysis</subject><ispartof>Biochemical and biophysical research communications, 1980-12, Vol.97 (4), p.1467-1473</ispartof><rights>1980 Academic Press, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c360t-5ddd8c9898c06637c1558501c399accd099fb5d64b6b9711d43ffa4a762c44163</citedby><cites>FETCH-LOGICAL-c360t-5ddd8c9898c06637c1558501c399accd099fb5d64b6b9711d43ffa4a762c44163</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-291X(80)80030-1$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7213371$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Clark, Robert D.</creatorcontrib><creatorcontrib>MacDonald, Russell E.</creatorcontrib><title>Enzyme crypticity as an indicator of membrane orientation in envelope vesicles from halobacteria</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>A membrane fraction prepared by freeze-thawing envelope vesicles from
Halobacterium halobium exhibits menadione-dependent NADH dehydrogenase activity (EC 1.6.9.9.3). The activity is “unmasked” by Triton X-100. Activity in freeze-thawed membrane preparations is more firmly membrane-bound than in sonicated vesicle preparations. Affinity for NADH is higher than in untreated vesicles and pyridine adenine dinucleotide specificity is the same. The data indicate that freeze-thawing causes reintegration of an adsorbed, extrinsic form of the dehydrogenase to yield an intrinsic, more native-like form of the enzyme. It is concluded that the extrinsic NADH dehydrogenase activity in vesicle preparations is not directly related to vesicle orientation.</description><subject>Cell Membrane - enzymology</subject><subject>Cell Membrane - ultrastructure</subject><subject>Freezing</subject><subject>Halobacterium - enzymology</subject><subject>Halobacterium - ultrastructure</subject><subject>NADH, NADPH Oxidoreductases - analysis</subject><subject>Octoxynol</subject><subject>Polyethylene Glycols</subject><subject>Quinone Reductases - analysis</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEFv1DAQhS0EKtvCT6jkE4JD6MwmduITQlWhSJV6oJW4GWc8EUZJvNjelZZfT7a76pXTHN5782Y-IS4RPiKgvvoOALpaG_zxvoMPHUANFb4QKwQD1RqheSlWz5bX4jzn3wCIjTZn4qxdY123uBI_b-a_-4klpf2mBAplL12WbpZh9oFciUnGQU489cnNLGMKPBdXQjw4JM87HuOG5Y5zoJGzHFKc5C83xt5R4RTcG_FqcGPmt6d5IR6_3Dxc31Z391-_XX--q6jWUCrlve_IdKYj0LpuCZXqFCDVxjgiD8YMvfK66XVvWkTf1MPgGtfqNTUN6vpCvDvu3aT4Z8u52Clk4nFczo7bbFvVKIVaLUZ1NFKKOSce7CaFyaW9RbAHsvaJrD1gsx3YJ7IWl9zlqWDbT-yfUyeUi_7pqPPy5S5wspkWWMQ-JKZifQz_afgHlZ2JnQ</recordid><startdate>19801231</startdate><enddate>19801231</enddate><creator>Clark, Robert D.</creator><creator>MacDonald, Russell E.</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>19801231</creationdate><title>Enzyme crypticity as an indicator of membrane orientation in envelope vesicles from halobacteria</title><author>Clark, Robert D. ; MacDonald, Russell E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c360t-5ddd8c9898c06637c1558501c399accd099fb5d64b6b9711d43ffa4a762c44163</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Cell Membrane - enzymology</topic><topic>Cell Membrane - ultrastructure</topic><topic>Freezing</topic><topic>Halobacterium - enzymology</topic><topic>Halobacterium - ultrastructure</topic><topic>NADH, NADPH Oxidoreductases - analysis</topic><topic>Octoxynol</topic><topic>Polyethylene Glycols</topic><topic>Quinone Reductases - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Clark, Robert D.</creatorcontrib><creatorcontrib>MacDonald, Russell E.</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>Clark, Robert D.</au><au>MacDonald, Russell E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzyme crypticity as an indicator of membrane orientation in envelope vesicles from halobacteria</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1980-12-31</date><risdate>1980</risdate><volume>97</volume><issue>4</issue><spage>1467</spage><epage>1473</epage><pages>1467-1473</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>A membrane fraction prepared by freeze-thawing envelope vesicles from
Halobacterium halobium exhibits menadione-dependent NADH dehydrogenase activity (EC 1.6.9.9.3). The activity is “unmasked” by Triton X-100. Activity in freeze-thawed membrane preparations is more firmly membrane-bound than in sonicated vesicle preparations. Affinity for NADH is higher than in untreated vesicles and pyridine adenine dinucleotide specificity is the same. The data indicate that freeze-thawing causes reintegration of an adsorbed, extrinsic form of the dehydrogenase to yield an intrinsic, more native-like form of the enzyme. It is concluded that the extrinsic NADH dehydrogenase activity in vesicle preparations is not directly related to vesicle orientation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7213371</pmid><doi>10.1016/S0006-291X(80)80030-1</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1980-12, Vol.97 (4), p.1467-1473 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Cell Membrane - enzymology Cell Membrane - ultrastructure Freezing Halobacterium - enzymology Halobacterium - ultrastructure NADH, NADPH Oxidoreductases - analysis Octoxynol Polyethylene Glycols Quinone Reductases - analysis |
| title | Enzyme crypticity as an indicator of membrane orientation in envelope vesicles from halobacteria |
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