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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6 Pt 1
|
| pubmed:dateCreated |
1994-2-8
|
| pubmed:abstractText |
The gastric proton pump, H(+)-K(+)-ATPase, is composed of alpha- and beta-subunits. The 95-kDa alpha-subunit has been referred to as the catalytic subunit containing sites for ATP binding and phosphorylation. The beta-subunit is a glycoprotein with a 34-kDa core peptide that has a single transmembrane segment, a small cytoplasmic NH2-terminal, and a large extracellular COOH-terminal domain with seven potential N-linked glycosylation sites. To further study the beta-subunit, we developed monoclonal antibodies that identified a 52-kDa mannose-rich glycoprotein that was deglycosylated by endoglycosidase H such that six transient intermediates were identified, as well as a 34-kDa beta-subunit core peptide. These observations suggest that the beta-subunit is synthesized as a 52-kDa glycoprotein with seven N-linked precursor high-mannose oligosaccharides that mature into complex oligosaccharides. One antibody, 2G11, inhibits the K(+)-stimulated ATP hydrolysis as well as K(+)-stimulated p-nitrophenyl phosphatase (pNPPase) activity of the H(+)-K(+)-ATPase. Kinetic studies revealed that 2G11 inhibited maximum velocity (Vmax) of ATP hydrolysis by approximately 50% with no change in the Km for K+, whereas, for pNPPase both Vmax and Km were altered. These studies demonstrate a functional role for the beta-subunit in the H(+)-K(+)-ATPase activity, especially the K(+)-induced conformational states.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-Nitrophenylphosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Cyanogen Bromide,
http://linkedlifedata.com/resource/pubmed/chemical/H( )-K( )-Exchanging ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0002-9513
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
265
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
C1562-70
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:8279517-4-Nitrophenylphosphatase,
pubmed-meshheading:8279517-Animals,
pubmed-meshheading:8279517-Antibodies, Monoclonal,
pubmed-meshheading:8279517-Blotting, Western,
pubmed-meshheading:8279517-Cyanogen Bromide,
pubmed-meshheading:8279517-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:8279517-Gastric Mucosa,
pubmed-meshheading:8279517-Glycosylation,
pubmed-meshheading:8279517-H(+)-K(+)-Exchanging ATPase,
pubmed-meshheading:8279517-Immunohistochemistry,
pubmed-meshheading:8279517-Kinetics,
pubmed-meshheading:8279517-Macromolecular Substances,
pubmed-meshheading:8279517-Membrane Glycoproteins,
pubmed-meshheading:8279517-Mice,
pubmed-meshheading:8279517-Mice, Inbred BALB C,
pubmed-meshheading:8279517-Microsomes,
pubmed-meshheading:8279517-Molecular Weight,
pubmed-meshheading:8279517-Peptide Fragments,
pubmed-meshheading:8279517-Potassium,
pubmed-meshheading:8279517-Rabbits,
pubmed-meshheading:8279517-Swine
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
Characterization of the beta-subunit of the H(+)-K(+)-ATPase using an inhibitory monoclonal antibody.
|
| pubmed:affiliation |
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|