| pubmed-article:3519316 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3519316 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
| pubmed-article:3519316 | lifeskim:mentions | umls-concept:C0030940 | lld:lifeskim |
| pubmed-article:3519316 | lifeskim:mentions | umls-concept:C0033628 | lld:lifeskim |
| pubmed-article:3519316 | lifeskim:mentions | umls-concept:C0035031 | lld:lifeskim |
| pubmed-article:3519316 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:3519316 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:3519316 | lifeskim:mentions | umls-concept:C2825492 | lld:lifeskim |
| pubmed-article:3519316 | lifeskim:mentions | umls-concept:C1882074 | lld:lifeskim |
| pubmed-article:3519316 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3519316 | pubmed:dateCreated | 1986-7-7 | lld:pubmed |
| pubmed-article:3519316 | pubmed:abstractText | The susceptibility of porcine relaxin and 125I-polytyrosyl-porcine relaxin to degradation by 3 purified enzymes involved in the degradation of insulin and proinsulin was examined. Rat liver glutathione-insulin transhydrogenase (GIT), which cleaves disulfide bonds in insulin, catalyzed a time- and concentration-dependent increase in trichloroacetic acid (TCA)-soluble radioactivity of relaxin. The Sephadex G-50 profile of the reaction products revealed conversion to the A- and B-chains. Relaxin competitively inhibited the degradation of insulin by GIT; however, kinetic analysis revealed insulin to be preferred over relaxin as a substrate. Rat liver cytosol neutral thiol peptidase (NTP) catalyzed a time- and concentration-dependent increase in the TCA solubility of relaxin and a shift in the Sephadex G-50 radioactivity profile to low molecular weight products. Kinetic analysis revealed that insulin and B-chain are preferred over relaxin as substrates for NTP. A third enzyme, rat kidney neutral metalloendopeptidase, which degrades proinsulin and insulin C-peptide but not insulin, also did not degrade porcine relaxin. | lld:pubmed |
| pubmed-article:3519316 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3519316 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3519316 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3519316 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3519316 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3519316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3519316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3519316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3519316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3519316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3519316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3519316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3519316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3519316 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3519316 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:3519316 | pubmed:issn | 0303-7207 | lld:pubmed |
| pubmed-article:3519316 | pubmed:author | pubmed-author:VarandaniP... | lld:pubmed |
| pubmed-article:3519316 | pubmed:author | pubmed-author:PilistineS... | lld:pubmed |
| pubmed-article:3519316 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3519316 | pubmed:volume | 46 | lld:pubmed |
| pubmed-article:3519316 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3519316 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3519316 | pubmed:pagination | 43-52 | lld:pubmed |
| pubmed-article:3519316 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:3519316 | pubmed:meshHeading | pubmed-meshheading:3519316-... | lld:pubmed |
| pubmed-article:3519316 | pubmed:meshHeading | pubmed-meshheading:3519316-... | lld:pubmed |
| pubmed-article:3519316 | pubmed:meshHeading | pubmed-meshheading:3519316-... | lld:pubmed |
| pubmed-article:3519316 | pubmed:meshHeading | pubmed-meshheading:3519316-... | lld:pubmed |
| pubmed-article:3519316 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3519316 | pubmed:articleTitle | Degradation of porcine relaxin by glutathione-insulin transhydrogenase and a neutral peptidase. | lld:pubmed |
| pubmed-article:3519316 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3519316 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3519316 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3519316 | lld:pubmed |
