| pubmed-article:3357339 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3357339 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
| pubmed-article:3357339 | lifeskim:mentions | umls-concept:C0026029 | lld:lifeskim |
| pubmed-article:3357339 | lifeskim:mentions | umls-concept:C0205070 | lld:lifeskim |
| pubmed-article:3357339 | lifeskim:mentions | umls-concept:C0405581 | lld:lifeskim |
| pubmed-article:3357339 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:3357339 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:3357339 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:3357339 | pubmed:dateCreated | 1988-5-20 | lld:pubmed |
| pubmed-article:3357339 | pubmed:abstractText | The activity of 4-ene-5 alpha-reductase was assayed in porcine testis homogenates and subcellular fractions, using testosterone as substrate. 'Marker' enzyme activities were utilized to indicate the purity of the subcellular fractions. 4-Ene-5 alpha-reductase activity was associated with the microsomal fraction; there was no activity in the purified nuclear fraction. Enzyme activity was higher in the testes of 6 week old pigs than those of 3 and 17 week old animals, and a range of activity was found. The enzyme was unstable when stored at -20 degrees C but the addition of albumin (0.1%, w/v) or glycerol (20%, v/v) to the buffer and storage at -70 degrees C or in liquid nitrogen ensured that maximal activity was retained for at least 35 days. In addition to 5 alpha-DHT, other 5 alpha-reduced metabolites and 4-androstenedione were formed in this reaction; NADPH was the preferred cofactor, but 40% of the 4-ene-5 alpha-reductase activity was retained when NADH was used. Solubilization of the microsomal enzyme was achieved using sodium citrate (0.1 M); 4-ene-5 alpha-reductase activity was enhanced to greater than 120% and 60% of this activity was in the soluble fraction. The optimum pH and temperature for both soluble and membrane-bound 4-ene-5 alpha-reductase were 6.9 and 32 degrees C, respectively. The mean apparent Km and Vmax were 0.6 mumol/l and 158 pmol/min/mg microsomal protein for the microsomal enzyme and 1.42 mumol/l and 212.0 pmol/min/mg soluble protein for the solubilized 4-ene-5 alpha-reductase. The estimated sedimentation coefficient was 11.6. | lld:pubmed |
| pubmed-article:3357339 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3357339 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3357339 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3357339 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3357339 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3357339 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3357339 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3357339 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3357339 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:3357339 | pubmed:issn | 0022-4731 | lld:pubmed |
| pubmed-article:3357339 | pubmed:author | pubmed-author:GowerD BDB | lld:pubmed |
| pubmed-article:3357339 | pubmed:author | pubmed-author:GoldringC ECE | lld:pubmed |
| pubmed-article:3357339 | pubmed:author | pubmed-author:WatkinsW JWJ | lld:pubmed |
| pubmed-article:3357339 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3357339 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:3357339 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3357339 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3357339 | pubmed:pagination | 325-31 | lld:pubmed |
| pubmed-article:3357339 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:3357339 | pubmed:meshHeading | pubmed-meshheading:3357339-... | lld:pubmed |
| pubmed-article:3357339 | pubmed:meshHeading | pubmed-meshheading:3357339-... | lld:pubmed |
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| pubmed-article:3357339 | pubmed:meshHeading | pubmed-meshheading:3357339-... | lld:pubmed |
| pubmed-article:3357339 | pubmed:meshHeading | pubmed-meshheading:3357339-... | lld:pubmed |
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| pubmed-article:3357339 | pubmed:meshHeading | pubmed-meshheading:3357339-... | lld:pubmed |
| pubmed-article:3357339 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3357339 | pubmed:articleTitle | Properties of 4-ene-5 alpha-reductase and studies on its solubilization from porcine testicular microsomes. | lld:pubmed |
| pubmed-article:3357339 | pubmed:affiliation | Division of Biochemistry, United Medical School (Guy's Hospital), London, England. | lld:pubmed |
| pubmed-article:3357339 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3357339 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:3357339 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
