| pubmed-article:1521330 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1521330 | lifeskim:mentions | umls-concept:C0030705 | lld:lifeskim |
| pubmed-article:1521330 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:1521330 | lifeskim:mentions | umls-concept:C0019874 | lld:lifeskim |
| pubmed-article:1521330 | lifeskim:mentions | umls-concept:C0036825 | lld:lifeskim |
| pubmed-article:1521330 | lifeskim:mentions | umls-concept:C0268632 | lld:lifeskim |
| pubmed-article:1521330 | lifeskim:mentions | umls-concept:C1539109 | lld:lifeskim |
| pubmed-article:1521330 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:1521330 | pubmed:dateCreated | 1992-10-9 | lld:pubmed |
| pubmed-article:1521330 | pubmed:abstractText | A specific polyclonal antiserum to human serum carnosinase was raised in rabbits and was used to prepare an agarose-protein A-antibody matrix. An antigen capture procedure showed that sera from homocarnosinosis patients, which lack carnosinase activity, contain an immunoreactive protein (M(r) 75,000) indistinguishable from the carnosinase band from normal serum. Other higher primates have active serum carnosinase and a similar immunoreactive M(r) 75,000 protein. The immunoaffinity matrix was used in a facile procedure to isolate pure carnosinase from human plasma with a yield of 69%. The antiserum inhibited human serum carnosinase strongly, but the maximum inhibition attained averaged only 71%. The antiserum inhibited human and chimpanzee serum carnosinases more effectively than gorilla or other higher primate serum carnosinases. | lld:pubmed |
| pubmed-article:1521330 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1521330 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1521330 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1521330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1521330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1521330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1521330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1521330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1521330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1521330 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1521330 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1521330 | pubmed:issn | 0009-8981 | lld:pubmed |
| pubmed-article:1521330 | pubmed:author | pubmed-author:LenneyJ FJF | lld:pubmed |
| pubmed-article:1521330 | pubmed:author | pubmed-author:JacksonM CMC | lld:pubmed |
| pubmed-article:1521330 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1521330 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:1521330 | pubmed:volume | 205 | lld:pubmed |
| pubmed-article:1521330 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1521330 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1521330 | pubmed:pagination | 109-16 | lld:pubmed |
| pubmed-article:1521330 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:meshHeading | pubmed-meshheading:1521330-... | lld:pubmed |
| pubmed-article:1521330 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1521330 | pubmed:articleTitle | Homocarnosinosis patients and great apes have a serum protein that cross-reacts with human serum carnosinase. | lld:pubmed |
| pubmed-article:1521330 | pubmed:affiliation | Pharmacology Department, School of Medicine, University of Hawaii, Honolulu 96822. | lld:pubmed |
| pubmed-article:1521330 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1521330 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
