Reconstitution of a heat shock effect in vitro: influence of GroE onthe thermal aggregation of alpha-glucosidase from yeast
alpha-Glucosidase from yeast is inactivated rapidly at temperatures above 42 degrees C. The thermal inactivation is accompanied by aggregation. The molecular chaperone GroEL suppresses the formation of aggregates by binding the thermally inactivated alpha-glucosidase. Spectroscopic studies suggest t...
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| Veröffentlicht in: | Biochemistry (Easton) 1991-12, Vol.30 (50) |
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| container_title | Biochemistry (Easton) |
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| creator | Holl-Neugebauer, B. (Boehringer Mannheim GmbH, Penzberg, Germany) Rudolph, R Schmidt, M Buchner, J |
| description | alpha-Glucosidase from yeast is inactivated rapidly at temperatures above 42 degrees C. The thermal inactivation is accompanied by aggregation. The molecular chaperone GroEL suppresses the formation of aggregates by binding the thermally inactivated alpha-glucosidase. Spectroscopic studies suggest that GroEL binds alpha-glucosidase in an intermediately folded state. The complex between alpha-glucosidase and GroEL can be dissolved by MgATP. GroES accelerates the MgATP-dependent dissociation of the alpha-glucosidase-GroEL complex. At elevated temperatures this release leads to the formation of aggregates, while at lower temperatures native, enzymatically active molecules are formed |
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(Boehringer Mannheim GmbH, Penzberg, Germany) ; Rudolph, R ; Schmidt, M ; Buchner, J</creator><creatorcontrib>Holl-Neugebauer, B. (Boehringer Mannheim GmbH, Penzberg, Germany) ; Rudolph, R ; Schmidt, M ; Buchner, J</creatorcontrib><description>alpha-Glucosidase from yeast is inactivated rapidly at temperatures above 42 degrees C. The thermal inactivation is accompanied by aggregation. The molecular chaperone GroEL suppresses the formation of aggregates by binding the thermally inactivated alpha-glucosidase. Spectroscopic studies suggest that GroEL binds alpha-glucosidase in an intermediately folded state. The complex between alpha-glucosidase and GroEL can be dissolved by MgATP. GroES accelerates the MgATP-dependent dissociation of the alpha-glucosidase-GroEL complex. At elevated temperatures this release leads to the formation of aggregates, while at lower temperatures native, enzymatically active molecules are formed</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><language>eng</language><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; AGOTAMIENTO POR EL CALOR ; CALOR ; CHALEUR ; COUP DE CHALEUR ; DENATURATION ; DESNATURALIZACION ; GLUCOSIDASA ; GLUCOSIDASE ; LEVADURA ; LEVURE ; RESISTANCE A LA TEMPERATURE ; RESISTENCIA A LA TEMPERATURA</subject><ispartof>Biochemistry (Easton), 1991-12, Vol.30 (50)</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids></links><search><creatorcontrib>Holl-Neugebauer, B. (Boehringer Mannheim GmbH, Penzberg, Germany)</creatorcontrib><creatorcontrib>Rudolph, R</creatorcontrib><creatorcontrib>Schmidt, M</creatorcontrib><creatorcontrib>Buchner, J</creatorcontrib><title>Reconstitution of a heat shock effect in vitro: influence of GroE onthe thermal aggregation of alpha-glucosidase from yeast</title><title>Biochemistry (Easton)</title><description>alpha-Glucosidase from yeast is inactivated rapidly at temperatures above 42 degrees C. The thermal inactivation is accompanied by aggregation. The molecular chaperone GroEL suppresses the formation of aggregates by binding the thermally inactivated alpha-glucosidase. Spectroscopic studies suggest that GroEL binds alpha-glucosidase in an intermediately folded state. The complex between alpha-glucosidase and GroEL can be dissolved by MgATP. GroES accelerates the MgATP-dependent dissociation of the alpha-glucosidase-GroEL complex. At elevated temperatures this release leads to the formation of aggregates, while at lower temperatures native, enzymatically active molecules are formed</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>AGOTAMIENTO POR EL CALOR</subject><subject>CALOR</subject><subject>CHALEUR</subject><subject>COUP DE CHALEUR</subject><subject>DENATURATION</subject><subject>DESNATURALIZACION</subject><subject>GLUCOSIDASA</subject><subject>GLUCOSIDASE</subject><subject>LEVADURA</subject><subject>LEVURE</subject><subject>RESISTANCE A LA TEMPERATURE</subject><subject>RESISTENCIA A LA TEMPERATURA</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><recordid>eNp9jM1qAkEQhIcQIRv1BXLqF1gYdVfZXIM_56hnacae2dFxOkzPCiEv7wrBo4ei6qOKelHFpJ7qsmqa-lUVWut5OW3m-k29i5x6rPSiKtTfNxmOkn3usucIbAGhJcwgLZszkLVkMvgIV58Tf_bJho6ioft0nXgJHHNL0CtdMAA6l8jh4yz8tFi60BkWf0QhsIkv8EsoeaQGFoPQ-N-H6mO13H1tSot8QJe8HPbbZlIvaj2bPS1v-KlI-A</recordid><startdate>19911217</startdate><enddate>19911217</enddate><creator>Holl-Neugebauer, B. 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(Boehringer Mannheim GmbH, Penzberg, Germany) ; Rudolph, R ; Schmidt, M ; Buchner, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-fao_agris_US91575033</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>AGOTAMIENTO POR EL CALOR</topic><topic>CALOR</topic><topic>CHALEUR</topic><topic>COUP DE CHALEUR</topic><topic>DENATURATION</topic><topic>DESNATURALIZACION</topic><topic>GLUCOSIDASA</topic><topic>GLUCOSIDASE</topic><topic>LEVADURA</topic><topic>LEVURE</topic><topic>RESISTANCE A LA TEMPERATURE</topic><topic>RESISTENCIA A LA TEMPERATURA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Holl-Neugebauer, B. (Boehringer Mannheim GmbH, Penzberg, Germany)</creatorcontrib><creatorcontrib>Rudolph, R</creatorcontrib><creatorcontrib>Schmidt, M</creatorcontrib><creatorcontrib>Buchner, J</creatorcontrib><collection>AGRIS</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Holl-Neugebauer, B. (Boehringer Mannheim GmbH, Penzberg, Germany)</au><au>Rudolph, R</au><au>Schmidt, M</au><au>Buchner, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reconstitution of a heat shock effect in vitro: influence of GroE onthe thermal aggregation of alpha-glucosidase from yeast</atitle><jtitle>Biochemistry (Easton)</jtitle><date>1991-12-17</date><risdate>1991</risdate><volume>30</volume><issue>50</issue><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>alpha-Glucosidase from yeast is inactivated rapidly at temperatures above 42 degrees C. The thermal inactivation is accompanied by aggregation. The molecular chaperone GroEL suppresses the formation of aggregates by binding the thermally inactivated alpha-glucosidase. Spectroscopic studies suggest that GroEL binds alpha-glucosidase in an intermediately folded state. The complex between alpha-glucosidase and GroEL can be dissolved by MgATP. GroES accelerates the MgATP-dependent dissociation of the alpha-glucosidase-GroEL complex. At elevated temperatures this release leads to the formation of aggregates, while at lower temperatures native, enzymatically active molecules are formed</abstract></addata></record> |
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| ispartof | Biochemistry (Easton), 1991-12, Vol.30 (50) |
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| source | American Chemical Society |
| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE AGOTAMIENTO POR EL CALOR CALOR CHALEUR COUP DE CHALEUR DENATURATION DESNATURALIZACION GLUCOSIDASA GLUCOSIDASE LEVADURA LEVURE RESISTANCE A LA TEMPERATURE RESISTENCIA A LA TEMPERATURA |
| title | Reconstitution of a heat shock effect in vitro: influence of GroE onthe thermal aggregation of alpha-glucosidase from yeast |
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