| pubmed-article:10353718 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10353718 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:10353718 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:10353718 | lifeskim:mentions | umls-concept:C1621574 | lld:lifeskim |
| pubmed-article:10353718 | lifeskim:mentions | umls-concept:C0597484 | lld:lifeskim |
| pubmed-article:10353718 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:10353718 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:10353718 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:10353718 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:10353718 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:10353718 | pubmed:dateCreated | 1999-8-5 | lld:pubmed |
| pubmed-article:10353718 | pubmed:abstractText | The Na+/H+ exchanger is a pH regulatory protein that is responsible for removal of excess intracellular protons in exchange for extracellular Na+. It is a plasma membrane protein with a large cytoplasmic carboxyl terminal domain that regulates activity of the membrane domain. We overexpressed and purified the cytoplasmic domain that was produced in Escherichia coli. This region (516-815 amino acids) was under control of the tac promoter from the plasmid pGEX-KG and was fused with glutathione S-transferase. Upon induction, the fusion protein was principally found in inclusion bodies. Purified inclusion bodies were solubilized and fractionated using preparative SDS polyacrylamide gel electrophoresis. To obtain free Na+/H+ exchanger protein the fusion protein was dialyzed against cleavage buffer and cleaved at the thrombin cleavage site between glutathione S-transferase and the Na+/H+ exchanger domain. Free Na+/H+ exchanger protein was obtained by rerunning the sample on preparative gel electrophoresis. The final yield of the purified protein was 2.15 mg protein/L of cell culture. After exhaustive dialysis the secondary structure of the purified protein was assessed using circular dichroism spectroscopy. The results indicated that the protein was 35% alpha-helix, 17% beta-turn, and 48% random coil. They suggest that the cytoplasmic domain is structured and some regions may be compact in nature. | lld:pubmed |
| pubmed-article:10353718 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10353718 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10353718 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10353718 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10353718 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10353718 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10353718 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10353718 | pubmed:issn | 0829-8211 | lld:pubmed |
| pubmed-article:10353718 | pubmed:author | pubmed-author:FliegelLL | lld:pubmed |
| pubmed-article:10353718 | pubmed:author | pubmed-author:RajarathnamKK | lld:pubmed |
| pubmed-article:10353718 | pubmed:author | pubmed-author:Gebreselassie... | lld:pubmed |
| pubmed-article:10353718 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10353718 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:10353718 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10353718 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10353718 | pubmed:pagination | 837-42 | lld:pubmed |
| pubmed-article:10353718 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10353718 | pubmed:meshHeading | pubmed-meshheading:10353718... | lld:pubmed |
| pubmed-article:10353718 | pubmed:meshHeading | pubmed-meshheading:10353718... | lld:pubmed |
| pubmed-article:10353718 | pubmed:meshHeading | pubmed-meshheading:10353718... | lld:pubmed |
| pubmed-article:10353718 | pubmed:meshHeading | pubmed-meshheading:10353718... | lld:pubmed |
| pubmed-article:10353718 | pubmed:meshHeading | pubmed-meshheading:10353718... | lld:pubmed |
| pubmed-article:10353718 | pubmed:meshHeading | pubmed-meshheading:10353718... | lld:pubmed |
| pubmed-article:10353718 | pubmed:meshHeading | pubmed-meshheading:10353718... | lld:pubmed |
| pubmed-article:10353718 | pubmed:meshHeading | pubmed-meshheading:10353718... | lld:pubmed |
| pubmed-article:10353718 | pubmed:meshHeading | pubmed-meshheading:10353718... | lld:pubmed |
| pubmed-article:10353718 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:10353718 | pubmed:articleTitle | Expression, purification, and characterization of the carboxyl-terminal region of the Na+/H+ exchanger. | lld:pubmed |
| pubmed-article:10353718 | pubmed:affiliation | Department of Biochemistry, University of Alberta, Edmonton, Canada. | lld:pubmed |
| pubmed-article:10353718 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10353718 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10353718 | lld:pubmed |
