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Article: Chemical modification of gastric microsomal potassium-stimulated ATPase
Title | Chemical modification of gastric microsomal potassium-stimulated ATPase |
---|---|
Authors | |
Keywords | (Gastric Microsome) Chemical Modification Fluorescent Labeling H + Transport K +-Stimulated Atpase |
Issue Date | 1980 |
Publisher | Elsevier 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? |
Abstract | Selective 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 Identifier | http://hdl.handle.net/10722/171475 |
ISSN | 2023 Impact Factor: 2.8 2023 SCImago Journal Rankings: 0.947 |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, HC | en_US |
dc.contributor.author | Forte, JG | en_US |
dc.date.accessioned | 2012-10-30T06:15:21Z | - |
dc.date.available | 2012-10-30T06:15:21Z | - |
dc.date.issued | 1980 | en_US |
dc.identifier.citation | Bba - Biomembranes, 1980, v. 598 n. 3, p. 595-605 | en_US |
dc.identifier.issn | 0005-2736 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/171475 | - |
dc.description.abstract | Selective 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.language | eng | en_US |
dc.publisher | Elsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbamem | en_US |
dc.relation.ispartof | BBA - Biomembranes | en_US |
dc.subject | (Gastric Microsome) | en_US |
dc.subject | Chemical Modification | en_US |
dc.subject | Fluorescent Labeling | en_US |
dc.subject | H + Transport | en_US |
dc.subject | K +-Stimulated Atpase | en_US |
dc.title | Chemical modification of gastric microsomal potassium-stimulated ATPase | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lee, HC:leehc@hku.hk | en_US |
dc.identifier.authority | Lee, HC=rp00545 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.scopus | eid_2-s2.0-0019318029 | en_US |
dc.identifier.volume | 598 | en_US |
dc.identifier.issue | 3 | en_US |
dc.identifier.spage | 595 | en_US |
dc.identifier.epage | 605 | en_US |
dc.identifier.isi | WOS:A1980JY83400017 | - |
dc.publisher.place | Netherlands | en_US |
dc.identifier.scopusauthorid | Lee, HC=26642959100 | en_US |
dc.identifier.scopusauthorid | Forte, JG=26425932500 | en_US |
dc.identifier.issnl | 0005-2736 | - |