pubmed-article:214450 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:214450 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
pubmed-article:214450 | lifeskim:mentions | umls-concept:C0014239 | lld:lifeskim |
pubmed-article:214450 | lifeskim:mentions | umls-concept:C0018042 | lld:lifeskim |
pubmed-article:214450 | lifeskim:mentions | umls-concept:C0005516 | lld:lifeskim |
pubmed-article:214450 | lifeskim:mentions | umls-concept:C0444504 | lld:lifeskim |
pubmed-article:214450 | pubmed:issue | 2 Pt 1 | lld:pubmed |
pubmed-article:214450 | pubmed:dateCreated | 1979-2-26 | lld:pubmed |
pubmed-article:214450 | pubmed:abstractText | NADPH cytochrome c (cyt c) reductase and glucose-6-phosphatase, two enzymes thought to be restricted to the endoplasmic reticulum (ER) and widely used as ER markers, are present in isolated Golgi fractions assayed immediately after their isolation. Both enzymes are rapidly inactivated in fractions stored at 0 degrees C in 0.25 M sucrose, conditions which do not affect the activity of other enzymes in the same preparation. The inactivation process was shown to be dependent on time and protein concentration and could be prevented by EDTA and catalase. Morphological evidence shows that extensive membrane damage occurs parallel with the inactivation. Taken together with the immunological data in the companion paper, the findings indicate that the enzymes NADPH cyt c reductase and probably glucose-6-phosphate are indigenous components of Golgi membranes. | lld:pubmed |
pubmed-article:214450 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:214450 | pubmed:language | eng | lld:pubmed |
pubmed-article:214450 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:214450 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:214450 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:214450 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:214450 | pubmed:month | Nov | lld:pubmed |
pubmed-article:214450 | pubmed:issn | 0021-9525 | lld:pubmed |
pubmed-article:214450 | pubmed:author | pubmed-author:ItoAA | lld:pubmed |
pubmed-article:214450 | pubmed:author | pubmed-author:PaladeG EGE | lld:pubmed |
pubmed-article:214450 | pubmed:author | pubmed-author:HowellK EKE | lld:pubmed |
pubmed-article:214450 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:214450 | pubmed:volume | 79 | lld:pubmed |
pubmed-article:214450 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:214450 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:214450 | pubmed:pagination | 581-9 | lld:pubmed |
pubmed-article:214450 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:214450 | pubmed:year | 1978 | lld:pubmed |
pubmed-article:214450 | pubmed:articleTitle | Endoplasmic reticulum marker enzymes in Golgi fractions--what does this mean? | lld:pubmed |
pubmed-article:214450 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:214450 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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