| pubmed-article:4377207 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:4377207 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
| pubmed-article:4377207 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:4377207 | lifeskim:mentions | umls-concept:C0022646 | lld:lifeskim |
| pubmed-article:4377207 | lifeskim:mentions | umls-concept:C0018042 | lld:lifeskim |
| pubmed-article:4377207 | lifeskim:mentions | umls-concept:C0017776 | lld:lifeskim |
| pubmed-article:4377207 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:4377207 | pubmed:dateCreated | 1975-10-30 | lld:pubmed |
| pubmed-article:4377207 | pubmed:abstractText | Subcellular fractions were prepared from mouse kidney homogenates by differential and sucrose-gradient centrifugation. A fraction enriched in Golgi apparatus was obtained, which had considerably enriched galactosyltransferase and thiamin pyrophosphatase activities, and was morphologically typical of Golgi material. This preparation also had high beta-glucuronidase activity, which increased concomitantly with microsomal beta-glucuronidase activity during the specific stimulation of the enzyme in male mouse kidney after androgen administration. The degree of stimulation was much greater in the Golgi fraction. Gel-electrophoretic patterns of Golgi beta-glucuronidase resembled more closely those of the enzyme located within lysosomes, but contained minor bands similar to those described previously (Swank & Paigen, 1973) as characteristic of the microsomal enzyme. It was concluded that the Golgi complex is involved in the distribution of the enzyme after its synthesis to both lysosomal and microsomal fractions. | lld:pubmed |
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| pubmed-article:4377207 | pubmed:language | eng | lld:pubmed |
| pubmed-article:4377207 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4377207 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:4377207 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:4377207 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:4377207 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:4377207 | pubmed:author | pubmed-author:MarshC ACA | lld:pubmed |
| pubmed-article:4377207 | pubmed:author | pubmed-author:LinC WCW | lld:pubmed |
| pubmed-article:4377207 | pubmed:author | pubmed-author:FishmanW HWH | lld:pubmed |
| pubmed-article:4377207 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:4377207 | pubmed:volume | 142 | lld:pubmed |
| pubmed-article:4377207 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:4377207 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:4377207 | pubmed:pagination | 491-7 | lld:pubmed |
| pubmed-article:4377207 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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| pubmed-article:4377207 | pubmed:year | 1974 | lld:pubmed |
| pubmed-article:4377207 | pubmed:articleTitle | Golgi beta-glucuronidase of androgen-stimulated mouse kidney. | lld:pubmed |
| pubmed-article:4377207 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4377207 | lld:pubmed |
