| pubmed-article:8346680 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8346680 | lifeskim:mentions | umls-concept:C0178453 | lld:lifeskim |
| pubmed-article:8346680 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:8346680 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8346680 | lifeskim:mentions | umls-concept:C0660482 | lld:lifeskim |
| pubmed-article:8346680 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:8346680 | pubmed:dateCreated | 1993-9-8 | lld:pubmed |
| pubmed-article:8346680 | pubmed:abstractText | Aminopeptidase yspI was purified to apparent homogeneity from the fission yeast Schizosaccharomyces pombe. The molecular mass of the native enzyme was estimated to be 184 kDa by gel filtration chromatography. A value of 92 kDa was calculated after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme is thus a dimer with two identical subunits. Optimum pH for cleavage of synthetic aminoacyl-4-nitroanilides is 7.0. Mercury ions, EDTA and chloroquine were found to be potent inhibitors of aminopeptidase yspI activity. Substrate specificity studies indicate that the purified enzyme cleaves L-lysine-4-nitroanilide with high efficiency. | lld:pubmed |
| pubmed-article:8346680 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8346680 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8346680 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8346680 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8346680 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8346680 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8346680 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8346680 | pubmed:issn | 0749-503X | lld:pubmed |
| pubmed-article:8346680 | pubmed:author | pubmed-author:ValliAA | lld:pubmed |
| pubmed-article:8346680 | pubmed:author | pubmed-author:Suárez-Rendue... | lld:pubmed |
| pubmed-article:8346680 | pubmed:author | pubmed-author:ArbesúM JMJ | lld:pubmed |
| pubmed-article:8346680 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8346680 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:8346680 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8346680 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8346680 | pubmed:pagination | 637-44 | lld:pubmed |
| pubmed-article:8346680 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8346680 | pubmed:meshHeading | pubmed-meshheading:8346680-... | lld:pubmed |
| pubmed-article:8346680 | pubmed:meshHeading | pubmed-meshheading:8346680-... | lld:pubmed |
| pubmed-article:8346680 | pubmed:meshHeading | pubmed-meshheading:8346680-... | lld:pubmed |
| pubmed-article:8346680 | pubmed:meshHeading | pubmed-meshheading:8346680-... | lld:pubmed |
| pubmed-article:8346680 | pubmed:meshHeading | pubmed-meshheading:8346680-... | lld:pubmed |
| pubmed-article:8346680 | pubmed:meshHeading | pubmed-meshheading:8346680-... | lld:pubmed |
| pubmed-article:8346680 | pubmed:meshHeading | pubmed-meshheading:8346680-... | lld:pubmed |
| pubmed-article:8346680 | pubmed:meshHeading | pubmed-meshheading:8346680-... | lld:pubmed |
| pubmed-article:8346680 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8346680 | pubmed:articleTitle | Purification and characterization of aminopeptidase yspI from Schizosaccharomyces pombe. | lld:pubmed |
| pubmed-article:8346680 | pubmed:affiliation | Departamento de Biologia Funcional, Facultad de Medicina, Universidad de Oviedo, Spain. | lld:pubmed |
| pubmed-article:8346680 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8346680 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
