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Change in target molecular size of the red beet plasma membrane ATPase during solubilization and reconstitution

The plasma membrane ATPase from red beet (Beta vulgaris L.) storage tissue associated with either native plasma membrane vesicles, a detergent-solubilized enzyme preparation or reconstituted liposomes was subjected to radiation inactivation analysis to determine if changes in target molecular size o...

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Published in:	Plant physiology (Bethesda) 1989-06, Vol.90 (2), p.394-397
Main Authors:	Briskin, D.P. (University of Illinois, Urbana, IL), Reynolds-Niesman, I
Format:	Article
Language:	English
Subjects:	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Adenosine triphosphatases Beets BETA VULGARIS Biological and medical sciences Braking radiation Cell membranes Cell physiology Chemical suspensions Communications Detergents Enzymes ESTRUCTURA CELULAR Fundamental and applied biological sciences. Psychology HIDROLASAS HIDROLISIS HYDROLASE HYDROLYSE INHIBIDORES DE ENZIMAS INHIBITEUR D'ENZYME Irradiation Membranes and Bioenergetics PESO MOLECULAR Plant physiology and development Plasma membrane and permeation POIDS MOLECULAIRE RADIACION GAMMA Radiation dosage RAYONNEMENT GAMMA Solubilization STRUCTURE CELLULAIRE
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container_title	Plant physiology (Bethesda)
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creator	Briskin, D.P. (University of Illinois, Urbana, IL) Reynolds-Niesman, I
description	The plasma membrane ATPase from red beet (Beta vulgaris L.) storage tissue associated with either native plasma membrane vesicles, a detergent-solubilized enzyme preparation or reconstituted liposomes was subjected to radiation inactivation analysis to determine if changes in target molecular size occurred with modification of its amphipathic environment. For each preparation of the enzyme, the decline in ATP hydrolytic activity with increasing dose of gamma-ray radiation demonstrated a simple exponential profile indicating the presence of a single target size. Analysis of the radiation inactivation profiles for the plasma membrane associated, solubilized, and reconstituted enzyme revealed target molecular sizes of 225 kilodaltons (kD), 129 kD, and 218 kD, respectively. These results suggest that the plasma membrane associated and reconstituted ATPase preparations consist of enzyme present as a dimer of 100 kD subunits while the solubilized enzyme is present in the monomeric form. These results also indicate that the 100 kD catalytic subunit most likely represents the minimal unit of ATP hydrolytic activity
doi_str_mv	10.1104/pp.90.2.394
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Psychology ; HIDROLASAS ; HIDROLISIS ; HYDROLASE ; HYDROLYSE ; INHIBIDORES DE ENZIMAS ; INHIBITEUR D'ENZYME ; Irradiation ; Membranes and Bioenergetics ; PESO MOLECULAR ; Plant physiology and development ; Plasma membrane and permeation ; POIDS MOLECULAIRE ; RADIACION GAMMA ; Radiation dosage ; RAYONNEMENT GAMMA ; Solubilization ; STRUCTURE CELLULAIRE</subject><ispartof>Plant physiology (Bethesda), 1989-06, Vol.90 (2), p.394-397</ispartof><rights>Copyright 1989 American Society of Plant Physiologists</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c480t-b9ed755a146a466cf6b681b25574e871ecded57cb5fa4cdb2d93ef1df3d45fe93</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4272091$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4272091$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,885,27915,27916,58229,58462</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6647509$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16666782$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Briskin, D.P. (University of Illinois, Urbana, IL)</creatorcontrib><creatorcontrib>Reynolds-Niesman, I</creatorcontrib><title>Change in target molecular size of the red beet plasma membrane ATPase during solubilization and reconstitution</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>The plasma membrane ATPase from red beet (Beta vulgaris L.) storage tissue associated with either native plasma membrane vesicles, a detergent-solubilized enzyme preparation or reconstituted liposomes was subjected to radiation inactivation analysis to determine if changes in target molecular size occurred with modification of its amphipathic environment. For each preparation of the enzyme, the decline in ATP hydrolytic activity with increasing dose of gamma-ray radiation demonstrated a simple exponential profile indicating the presence of a single target size. Analysis of the radiation inactivation profiles for the plasma membrane associated, solubilized, and reconstituted enzyme revealed target molecular sizes of 225 kilodaltons (kD), 129 kD, and 218 kD, respectively. These results suggest that the plasma membrane associated and reconstituted ATPase preparations consist of enzyme present as a dimer of 100 kD subunits while the solubilized enzyme is present in the monomeric form. 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For each preparation of the enzyme, the decline in ATP hydrolytic activity with increasing dose of gamma-ray radiation demonstrated a simple exponential profile indicating the presence of a single target size. Analysis of the radiation inactivation profiles for the plasma membrane associated, solubilized, and reconstituted enzyme revealed target molecular sizes of 225 kilodaltons (kD), 129 kD, and 218 kD, respectively. These results suggest that the plasma membrane associated and reconstituted ATPase preparations consist of enzyme present as a dimer of 100 kD subunits while the solubilized enzyme is present in the monomeric form. These results also indicate that the 100 kD catalytic subunit most likely represents the minimal unit of ATP hydrolytic activity</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>16666782</pmid><doi>10.1104/pp.90.2.394</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record>
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source	JSTOR Archival Journals and Primary Sources Collection; Alma/SFX Local Collection
subjects	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Adenosine triphosphatases Beets BETA VULGARIS Biological and medical sciences Braking radiation Cell membranes Cell physiology Chemical suspensions Communications Detergents Enzymes ESTRUCTURA CELULAR Fundamental and applied biological sciences. Psychology HIDROLASAS HIDROLISIS HYDROLASE HYDROLYSE INHIBIDORES DE ENZIMAS INHIBITEUR D'ENZYME Irradiation Membranes and Bioenergetics PESO MOLECULAR Plant physiology and development Plasma membrane and permeation POIDS MOLECULAIRE RADIACION GAMMA Radiation dosage RAYONNEMENT GAMMA Solubilization STRUCTURE CELLULAIRE
title	Change in target molecular size of the red beet plasma membrane ATPase during solubilization and reconstitution
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