| pubmed-article:2148692 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2148692 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2148692 | lifeskim:mentions | umls-concept:C0032043 | lld:lifeskim |
| pubmed-article:2148692 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:2148692 | lifeskim:mentions | umls-concept:C0018440 | lld:lifeskim |
| pubmed-article:2148692 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:2148692 | lifeskim:mentions | umls-concept:C1549781 | lld:lifeskim |
| pubmed-article:2148692 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:2148692 | pubmed:issue | 48 | lld:pubmed |
| pubmed-article:2148692 | pubmed:dateCreated | 1991-2-28 | lld:pubmed |
| pubmed-article:2148692 | pubmed:abstractText | Transient exposure of human placental brush-border membrane vesicles to cholate reorients the ATP-driven H+ pump, enabling the pump to transport H+ into the vesicles upon addition of ATP to the external medium. H+ uptake can be measured in these vesicles by following the decrease in the absorbance of acridine orange, a delta pH indicator. We investigated the role of tyrosyl residues in the catalytic function of the H+ pump by studying the effects of tyrosyl group specific reagents on ATP-driven H+ uptake in cholate-pretreated membrane vesicles. The reagents tested were 7-chloro-4-nitro-2,1,3-benzoxadiazole (NBD-Cl), N-acetylimidazole, tetranitromethane, and p-nitrobenzenesulfonyl fluoride. Treatment of the membrane vesicles with these reagents resulted in the inhibition of the ATP-driven H+ uptake, and the inhibitory potency was in the following order: NBD-Cl greater than tetranitromethane greater than p-nitrobenzenesulfonyl fluoride greater than N-acetylimidazole. The inhibition of the H+ pump by NBD-Cl was reversible by 2-mercaptoethanol, and the inhibition by N-acetylimidazole was reversible by hydroxylamine. Since these reagents are not absolutely specific for tyrosyl groups and can also react with thiol groups, we studied the interaction of N-acetylimidazole with the H+ pump whose triol groups were masked by reaction with p-(chloromercuri)benzenesulfonate. The SH-masked pump was totally inactive, but the activity could be restored by dithiothreitol. On the contrary, the activity of the SH-masked H+ pump which was subsequently treated with N-acetylimidazole could not be restored by dithiothreitol, suggesting that thiol groups were not involved in the inhibition of the H+ pump by N-acetylimidazole.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
| pubmed-article:2148692 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2148692 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2148692 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2148692 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2148692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2148692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2148692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2148692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2148692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2148692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2148692 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2148692 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2148692 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:2148692 | pubmed:author | pubmed-author:LeibachF HFH | lld:pubmed |
| pubmed-article:2148692 | pubmed:author | pubmed-author:BurckhardtGG | lld:pubmed |
| pubmed-article:2148692 | pubmed:author | pubmed-author:MaheshV BVB | lld:pubmed |
| pubmed-article:2148692 | pubmed:author | pubmed-author:GanapathyVV | lld:pubmed |
| pubmed-article:2148692 | pubmed:author | pubmed-author:KulanthaivelP... | lld:pubmed |
| pubmed-article:2148692 | pubmed:author | pubmed-author:SimonB JBJ | lld:pubmed |
| pubmed-article:2148692 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2148692 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:2148692 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:2148692 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2148692 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2148692 | pubmed:pagination | 10807-13 | lld:pubmed |
| pubmed-article:2148692 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:2148692 | pubmed:meshHeading | pubmed-meshheading:2148692-... | lld:pubmed |
| pubmed-article:2148692 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2148692 | pubmed:articleTitle | The ATP-binding site of the human placental H+ pump contains essential tyrosyl residues. | lld:pubmed |
| pubmed-article:2148692 | pubmed:affiliation | Department of Cell and Molecular Biology, Medical College of Georgia, Augusta 30912-2100. | lld:pubmed |
| pubmed-article:2148692 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2148692 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2148692 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2148692 | lld:pubmed |
