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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
31
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pubmed:dateCreated |
1989-11-28
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pubmed:abstractText |
Golgi apparatus was prepared from rat liver, and enzymatic properties and the subunit structure of the H+-ATPase were characterized. GTP (and also ITP) was found to drive H+-transport with about 20% of the initial velocity as that of ATP. Bafilomycin, a specific inhibitor for vacuolar H+-ATPase, inhibited the activity at 2.5 nM. The H+-ATPase was completely inhibited in the cold in the presence of MgATP (5 mM) and NaNO3 (0.1 M). The cold inactivation of the H+-ATPase resulted in release of a set of polypeptides from Golgi membrane, with molecular masses almost identical to that of the hydrophilic sector of chromaffin granule H+-ATPase (72, 57, 41, 34, and 33 kDa). Three of these polypeptides (72, 57, and 34 kDa), cross-reacted with antibodies against the corresponding subunits of the chromaffin granule H+-ATPase. A counterpart of the 39-kDa hydrophobic component of chromaffin granule H+-ATPase was identified in the membrane, but no 115-kDa component was found. Hence, the Golgi H+-ATPase shows typical features of vacuolar H+-ATPase, in relatively low substrate specificity, its response to inhibitors, inactivation by cold treatment in the presence of MgATP, and subunit composition judged by antibody cross-reactivity.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Macrolides,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrates,
http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/bafilomycin A,
http://linkedlifedata.com/resource/pubmed/chemical/sodium nitrate
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
264
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18445-50
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2530222-Adenosine Diphosphate,
pubmed-meshheading:2530222-Adenosine Triphosphate,
pubmed-meshheading:2530222-Animals,
pubmed-meshheading:2530222-Anti-Bacterial Agents,
pubmed-meshheading:2530222-Chromaffin Granules,
pubmed-meshheading:2530222-Cold Temperature,
pubmed-meshheading:2530222-Golgi Apparatus,
pubmed-meshheading:2530222-Guanosine Triphosphate,
pubmed-meshheading:2530222-Liver,
pubmed-meshheading:2530222-Macrolides,
pubmed-meshheading:2530222-Molecular Weight,
pubmed-meshheading:2530222-Nitrates,
pubmed-meshheading:2530222-Proton-Translocating ATPases,
pubmed-meshheading:2530222-Rats,
pubmed-meshheading:2530222-Vacuoles
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pubmed:year |
1989
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pubmed:articleTitle |
H+-translocating ATPase in Golgi apparatus. Characterization as vacuolar H+-ATPase and its subunit structures.
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pubmed:affiliation |
Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110.
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pubmed:publicationType |
Journal Article,
Comparative Study
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