| pubmed-article:2670924 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2670924 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2670924 | lifeskim:mentions | umls-concept:C0072249 | lld:lifeskim |
| pubmed-article:2670924 | lifeskim:mentions | umls-concept:C0302891 | lld:lifeskim |
| pubmed-article:2670924 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:2670924 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:2670924 | pubmed:dateCreated | 1989-10-11 | lld:pubmed |
| pubmed-article:2670924 | pubmed:abstractText | To clarify contradicting observations on the identity of inactive renin and prorenin, inactive renin was completely purified from native human chorion laeve and the culture medium of human chorion cells. A 720,000-fold purification with 14% recovery was achieved from chorion laeve in 6 steps, including immunoaffinity chromatography on a monoclonal antibody to human renin coupled to Protein A-Sepharose CL-4B. A 3,100-fold purification with 40% recovery was achieved from chorion culture medium in 4 steps, including immunoaffinity chromatography. Inactive renin purified from the two different sources migrated as a single protein band with the same molecular weight of 47,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and consisted of multiple components that could be resolved by isoelectric focusing. Both had the same pI values which shifted downward upon activation by trypsin; however, relative peak heights were different between the two preparations. The purified inactive renin from chorion laeve was completely inactive and did not bind to pepstatin-aminohexyl-Sepharose; however, that from chorion culture medium was partially active and completely bound to the pepstatin gel, indicating that each molecule is partially activated. Trypsin-activated inactive renins from both sources were identical with human renal renin in terms of pH optimum and Km. Specific activities of trypsin-activated inactive renin from chorion laeve and chorion culture medium were 529 Goldblatt units/mg of protein and 449 Goldblatt units/mg of protein, respectively. Amino acid sequence analysis of both of the purified inactive renin preparations demonstrated a leucine residue at the amino terminus. The sequence of 11 additional amino acids was identical in both and agreed with that predicted from the base sequence of the renin gene. These findings indicate that preprorenin is converted to prorenin following removal of a 23-amino acid signal peptide and that the native inactive renin, whose amino acid sequence commences with Leu-Pro-Thr..., is prorenin. | lld:pubmed |
| pubmed-article:2670924 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2670924 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2670924 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2670924 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2670924 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2670924 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2670924 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2670924 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2670924 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2670924 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2670924 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:2670924 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2670924 | pubmed:author | pubmed-author:PoisnerA MAM | lld:pubmed |
| pubmed-article:2670924 | pubmed:author | pubmed-author:InagamiTT | lld:pubmed |
| pubmed-article:2670924 | pubmed:author | pubmed-author:BoehmF HFH | lld:pubmed |
| pubmed-article:2670924 | pubmed:author | pubmed-author:MizunoKK | lld:pubmed |
| pubmed-article:2670924 | pubmed:author | pubmed-author:NakajoSS | lld:pubmed |
| pubmed-article:2670924 | pubmed:author | pubmed-author:MarcotteP APA | lld:pubmed |
| pubmed-article:2670924 | pubmed:author | pubmed-author:HollemanW HWH | lld:pubmed |
| pubmed-article:2670924 | pubmed:author | pubmed-author:EganD ADA | lld:pubmed |
| pubmed-article:2670924 | pubmed:author | pubmed-author:HeusserCC | lld:pubmed |
| pubmed-article:2670924 | pubmed:author | pubmed-author:HigashimoriKK | lld:pubmed |
| pubmed-article:2670924 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2670924 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:2670924 | pubmed:volume | 264 | lld:pubmed |
| pubmed-article:2670924 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2670924 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2670924 | pubmed:pagination | 14662-7 | lld:pubmed |
| pubmed-article:2670924 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2670924 | pubmed:meshHeading | pubmed-meshheading:2670924-... | lld:pubmed |
| pubmed-article:2670924 | pubmed:meshHeading | pubmed-meshheading:2670924-... | lld:pubmed |
| pubmed-article:2670924 | pubmed:meshHeading | pubmed-meshheading:2670924-... | lld:pubmed |
| pubmed-article:2670924 | pubmed:meshHeading | pubmed-meshheading:2670924-... | lld:pubmed |
| pubmed-article:2670924 | pubmed:meshHeading | pubmed-meshheading:2670924-... | lld:pubmed |
| pubmed-article:2670924 | pubmed:meshHeading | pubmed-meshheading:2670924-... | lld:pubmed |
| pubmed-article:2670924 | pubmed:meshHeading | pubmed-meshheading:2670924-... | lld:pubmed |
| pubmed-article:2670924 | pubmed:meshHeading | pubmed-meshheading:2670924-... | lld:pubmed |
| pubmed-article:2670924 | pubmed:meshHeading | pubmed-meshheading:2670924-... | lld:pubmed |
| pubmed-article:2670924 | pubmed:meshHeading | pubmed-meshheading:2670924-... | lld:pubmed |
| pubmed-article:2670924 | pubmed:meshHeading | pubmed-meshheading:2670924-... | lld:pubmed |
| pubmed-article:2670924 | pubmed:meshHeading | pubmed-meshheading:2670924-... | lld:pubmed |
| pubmed-article:2670924 | pubmed:meshHeading | pubmed-meshheading:2670924-... | lld:pubmed |
| pubmed-article:2670924 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2670924 | pubmed:articleTitle | Pure human inactive renin. Evidence that native inactive renin is prorenin. | lld:pubmed |
| pubmed-article:2670924 | pubmed:affiliation | Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232. | lld:pubmed |
| pubmed-article:2670924 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2670924 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
