| pubmed-article:8393961 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8393961 | lifeskim:mentions | umls-concept:C0034493 | lld:lifeskim |
| pubmed-article:8393961 | lifeskim:mentions | umls-concept:C0178523 | lld:lifeskim |
| pubmed-article:8393961 | lifeskim:mentions | umls-concept:C0442805 | lld:lifeskim |
| pubmed-article:8393961 | lifeskim:mentions | umls-concept:C2348822 | lld:lifeskim |
| pubmed-article:8393961 | lifeskim:mentions | umls-concept:C0681079 | lld:lifeskim |
| pubmed-article:8393961 | lifeskim:mentions | umls-concept:C0302891 | lld:lifeskim |
| pubmed-article:8393961 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8393961 | pubmed:dateCreated | 1993-9-3 | lld:pubmed |
| pubmed-article:8393961 | pubmed:abstractText | Experiments were designed to examine the effects of trypsin-mediated proteolysis on the activity of the rabbit renal brush border membrane Na(+)-H+ exchanger. Incubation of brush border membrane vesicles with trypsin resulted in a concentration and time-dependent change in proton gradient-stimulated sodium uptake. Extensive trypsin digestion resulted in a marked decrease in the activity of the transporter. By contrast, limited trypsin digestion resulted in a significant increase in proton gradient-stimulated, amiloride-inhibitable sodium uptake. Sodium-dependent proton efflux was also significantly increased by limited trypsin digestion. The passive permeability of the vesicles to sodium and protons, and the sodium-dependent and sodium-independent uptake of glucose were not affected by limited trypsin digestion. These data indicate that limited trypsin digestion increases the activity of the renal brush border membrane Na(+)-H+ exchanger. It is suggested that the renal Na(+)-H+ exchanger contains one or more inhibitory components or sites which are sensitive to inactivation by limited trypsin-mediated proteolysis. | lld:pubmed |
| pubmed-article:8393961 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8393961 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8393961 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8393961 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8393961 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8393961 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8393961 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8393961 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8393961 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8393961 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8393961 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8393961 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8393961 | pubmed:issn | 0378-0392 | lld:pubmed |
| pubmed-article:8393961 | pubmed:author | pubmed-author:WeinmanE JEJ | lld:pubmed |
| pubmed-article:8393961 | pubmed:author | pubmed-author:ShenolikarSS | lld:pubmed |
| pubmed-article:8393961 | pubmed:author | pubmed-author:SteplockD ADA | lld:pubmed |
| pubmed-article:8393961 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8393961 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:8393961 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8393961 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8393961 | pubmed:pagination | 47-50 | lld:pubmed |
| pubmed-article:8393961 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8393961 | pubmed:meshHeading | pubmed-meshheading:8393961-... | lld:pubmed |
| pubmed-article:8393961 | pubmed:meshHeading | pubmed-meshheading:8393961-... | lld:pubmed |
| pubmed-article:8393961 | pubmed:meshHeading | pubmed-meshheading:8393961-... | lld:pubmed |
| pubmed-article:8393961 | pubmed:meshHeading | pubmed-meshheading:8393961-... | lld:pubmed |
| pubmed-article:8393961 | pubmed:meshHeading | pubmed-meshheading:8393961-... | lld:pubmed |
| pubmed-article:8393961 | pubmed:meshHeading | pubmed-meshheading:8393961-... | lld:pubmed |
| pubmed-article:8393961 | pubmed:meshHeading | pubmed-meshheading:8393961-... | lld:pubmed |
| pubmed-article:8393961 | pubmed:meshHeading | pubmed-meshheading:8393961-... | lld:pubmed |
| pubmed-article:8393961 | pubmed:meshHeading | pubmed-meshheading:8393961-... | lld:pubmed |
| pubmed-article:8393961 | pubmed:meshHeading | pubmed-meshheading:8393961-... | lld:pubmed |
| pubmed-article:8393961 | pubmed:meshHeading | pubmed-meshheading:8393961-... | lld:pubmed |
| pubmed-article:8393961 | pubmed:meshHeading | pubmed-meshheading:8393961-... | lld:pubmed |
| pubmed-article:8393961 | pubmed:meshHeading | pubmed-meshheading:8393961-... | lld:pubmed |
| pubmed-article:8393961 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8393961 | pubmed:articleTitle | Trypsin digestion increases Na(+)-H+ exchange rates in native rabbit brush border membrane. | lld:pubmed |
| pubmed-article:8393961 | pubmed:affiliation | Department of Medicine, University of California, Los Angeles. | lld:pubmed |
| pubmed-article:8393961 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8393961 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:8393961 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8393961 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:8393961 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
