| pubmed-article:6616870 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6616870 | lifeskim:mentions | umls-concept:C1273518 | lld:lifeskim |
| pubmed-article:6616870 | lifeskim:mentions | umls-concept:C0007806 | lld:lifeskim |
| pubmed-article:6616870 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
| pubmed-article:6616870 | lifeskim:mentions | umls-concept:C0268632 | lld:lifeskim |
| pubmed-article:6616870 | lifeskim:mentions | umls-concept:C1457869 | lld:lifeskim |
| pubmed-article:6616870 | lifeskim:mentions | umls-concept:C1539109 | lld:lifeskim |
| pubmed-article:6616870 | lifeskim:mentions | umls-concept:C0062927 | lld:lifeskim |
| pubmed-article:6616870 | lifeskim:mentions | umls-concept:C0205250 | lld:lifeskim |
| pubmed-article:6616870 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:6616870 | pubmed:dateCreated | 1983-11-23 | lld:pubmed |
| pubmed-article:6616870 | pubmed:abstractText | Patients afflicted with homocarnosinosis have elevated concentrations of homocarnosine in brain and CSF. It has been reported that they lack brain homocarnosinase. However, we have found that these patients are deficient in serum carnosinase, a dipeptidase which hydrolyzes homocarnosine about 5% as rapidly as it splits carnosine. Homocarnosinase could not be detected in normal human brain extracts after isoelectric focusing or DEAE-cellulose column chromatography. The ability of brain extracts to hydrolyze homocarnosine thus appears to be attributable solely to the serum carnosinase which is present because of serum trapped in the brain sample. Preliminary data indicate that homocarnosinase is probably not present in 13 other human tissues. Normal CSF contained serum carnosinase, whereas the CSF of a homocarnosinosis patient was lacking this enzyme. Thus it appears that the elevated concentrations of homocarnosine in the CSF of homocarnosinosis patients are attributable to serum carnosinase deficiency. | lld:pubmed |
| pubmed-article:6616870 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6616870 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6616870 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6616870 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6616870 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6616870 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6616870 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6616870 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6616870 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6616870 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:6616870 | pubmed:issn | 0009-8981 | lld:pubmed |
| pubmed-article:6616870 | pubmed:author | pubmed-author:LenneyJ FJF | lld:pubmed |
| pubmed-article:6616870 | pubmed:author | pubmed-author:SjaastadOO | lld:pubmed |
| pubmed-article:6616870 | pubmed:author | pubmed-author:KuceraC MCM | lld:pubmed |
| pubmed-article:6616870 | pubmed:author | pubmed-author:PeppersS CSC | lld:pubmed |
| pubmed-article:6616870 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6616870 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:6616870 | pubmed:volume | 132 | lld:pubmed |
| pubmed-article:6616870 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6616870 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6616870 | pubmed:pagination | 157-65 | lld:pubmed |
| pubmed-article:6616870 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:6616870 | pubmed:meshHeading | pubmed-meshheading:6616870-... | lld:pubmed |
| pubmed-article:6616870 | pubmed:meshHeading | pubmed-meshheading:6616870-... | lld:pubmed |
| pubmed-article:6616870 | pubmed:meshHeading | pubmed-meshheading:6616870-... | lld:pubmed |
| pubmed-article:6616870 | pubmed:meshHeading | pubmed-meshheading:6616870-... | lld:pubmed |
| pubmed-article:6616870 | pubmed:meshHeading | pubmed-meshheading:6616870-... | lld:pubmed |
| pubmed-article:6616870 | pubmed:meshHeading | pubmed-meshheading:6616870-... | lld:pubmed |
| pubmed-article:6616870 | pubmed:meshHeading | pubmed-meshheading:6616870-... | lld:pubmed |
| pubmed-article:6616870 | pubmed:meshHeading | pubmed-meshheading:6616870-... | lld:pubmed |
| pubmed-article:6616870 | pubmed:meshHeading | pubmed-meshheading:6616870-... | lld:pubmed |
| pubmed-article:6616870 | pubmed:meshHeading | pubmed-meshheading:6616870-... | lld:pubmed |
| pubmed-article:6616870 | pubmed:meshHeading | pubmed-meshheading:6616870-... | lld:pubmed |
| pubmed-article:6616870 | pubmed:year | 1983 | lld:pubmed |
| pubmed-article:6616870 | pubmed:articleTitle | Homocarnosinosis: lack of serum carnosinase is the defect probably responsible for elevated brain and CSF homocarnosine. | lld:pubmed |
| pubmed-article:6616870 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:84735 | entrezgene:pubmed | pubmed-article:6616870 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6616870 | lld:pubmed |
