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Article: Chemical modification of gastric microsomal potassium-stimulated ATPase

TitleChemical modification of gastric microsomal potassium-stimulated ATPase
Authors
Keywords(Gastric Microsome)
Chemical Modification
Fluorescent Labeling
H + Transport
K +-Stimulated Atpase
Issue Date1980
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbamem
Citation
Bba - Biomembranes, 1980, v. 598 n. 3, p. 595-605 How to Cite?
AbstractSelective chemical modification was used to examine amino acid residues that might be critical for the operation of the gastric K +-stimulated ATPase. Modification of amino groups with the fluorigenic reagent 2-methoxy-2,4-diphenyl-3-dihydrofuranone resulted in selective inhibition of the K +-stimulated ATPase and H +-transporting activities of the gastric microsomes, while the Mg 2+-ATPase was not affected. Half-maximal inhibition occurred at about 3 μg 2-methoxy-2,4-diphenyl-3-dihydrofuranone/ml at pH 8.5. ATP provided complete protection against inhibition; the apparent K m for ATP protection was about 50 μM. Nucleotide selectivity for protection was ATP > ADP > ITP > GTP > CTP > AMP. Sodium dodecyl sulfate gel electrophoresis of the reacted microsomes showed that virtually all the fluorescent label was on the M r 100 000 peptide band, a very small peptide, and aminolipids. In the presence of ATP there was about 75% reduction in the fluorescent label on the M r 100 000 peptide, but no change in the labeling of the other components. The arginine specific reagent, butanedione, inhibited Mg 2+-ATPase and K +-ATPase activities, with the former being much less reactive. Similar to 2-methoxy-2,4-diphenyl-3-dihydrofuranone, ATP provided complete protection from butanedione treatment. It is concluded that amino and guanidino groups are critical to the function of the K +-ATPase and may be actually at the ATP binding site. © 1980.
Persistent Identifierhttp://hdl.handle.net/10722/171475
ISSN
2015 Impact Factor: 3.687
2015 SCImago Journal Rankings: 1.769

 

DC FieldValueLanguage
dc.contributor.authorLee, HCen_US
dc.contributor.authorForte, JGen_US
dc.date.accessioned2012-10-30T06:15:21Z-
dc.date.available2012-10-30T06:15:21Z-
dc.date.issued1980en_US
dc.identifier.citationBba - Biomembranes, 1980, v. 598 n. 3, p. 595-605en_US
dc.identifier.issn0005-2736en_US
dc.identifier.urihttp://hdl.handle.net/10722/171475-
dc.description.abstractSelective chemical modification was used to examine amino acid residues that might be critical for the operation of the gastric K +-stimulated ATPase. Modification of amino groups with the fluorigenic reagent 2-methoxy-2,4-diphenyl-3-dihydrofuranone resulted in selective inhibition of the K +-stimulated ATPase and H +-transporting activities of the gastric microsomes, while the Mg 2+-ATPase was not affected. Half-maximal inhibition occurred at about 3 μg 2-methoxy-2,4-diphenyl-3-dihydrofuranone/ml at pH 8.5. ATP provided complete protection against inhibition; the apparent K m for ATP protection was about 50 μM. Nucleotide selectivity for protection was ATP > ADP > ITP > GTP > CTP > AMP. Sodium dodecyl sulfate gel electrophoresis of the reacted microsomes showed that virtually all the fluorescent label was on the M r 100 000 peptide band, a very small peptide, and aminolipids. In the presence of ATP there was about 75% reduction in the fluorescent label on the M r 100 000 peptide, but no change in the labeling of the other components. The arginine specific reagent, butanedione, inhibited Mg 2+-ATPase and K +-ATPase activities, with the former being much less reactive. Similar to 2-methoxy-2,4-diphenyl-3-dihydrofuranone, ATP provided complete protection from butanedione treatment. It is concluded that amino and guanidino groups are critical to the function of the K +-ATPase and may be actually at the ATP binding site. © 1980.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbamemen_US
dc.relation.ispartofBBA - Biomembranesen_US
dc.subject(Gastric Microsome)en_US
dc.subjectChemical Modificationen_US
dc.subjectFluorescent Labelingen_US
dc.subjectH + Transporten_US
dc.subjectK +-Stimulated Atpaseen_US
dc.titleChemical modification of gastric microsomal potassium-stimulated ATPaseen_US
dc.typeArticleen_US
dc.identifier.emailLee, HC:leehc@hku.hken_US
dc.identifier.authorityLee, HC=rp00545en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.scopuseid_2-s2.0-0019318029en_US
dc.identifier.volume598en_US
dc.identifier.issue3en_US
dc.identifier.spage595en_US
dc.identifier.epage605en_US
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridLee, HC=26642959100en_US
dc.identifier.scopusauthoridForte, JG=26425932500en_US

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