| pubmed-article:14600395 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14600395 | lifeskim:mentions | umls-concept:C1882726 | lld:lifeskim |
| pubmed-article:14600395 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:14600395 | lifeskim:mentions | umls-concept:C0034307 | lld:lifeskim |
| pubmed-article:14600395 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:14600395 | lifeskim:mentions | umls-concept:C1440928 | lld:lifeskim |
| pubmed-article:14600395 | lifeskim:mentions | umls-concept:C0051655 | lld:lifeskim |
| pubmed-article:14600395 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:14600395 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:14600395 | pubmed:dateCreated | 2003-11-5 | lld:pubmed |
| pubmed-article:14600395 | pubmed:abstractText | Pyroglutamyl aminopeptidase I (PAP-I) is a cytosolic cysteine peptidase, which hydrolytically removes the L-pyroglutamate residue from the amino terminus of endogenous proteins and peptides. L-Pyroglutamyl p-nitroanilide serves as the synthetic substrate of this enzyme, while there is a possibility of other hydrolases being involved in the hydrolysis of this xenobiotic substrate. We cloned a full-length cDNA encoding rat PAP-I from a rat liver cDNA library and expressed this cDNA in Escherichia coli to obtain a recombinant PAP-I as a single protein. The cDNA encoded a sequence of 209 amino acids with a calculated molecular weight of 22913 Da. The homology of the deduced amino acid sequence of rat PAP-I was 98.6 and 94.3% to mouse and human PAP-Is, respectively. The biochemical properties of the recombinant rat PAP-I were almost identical to those of the recombinant mouse and human PAP-Is and the purified rat liver cytosolic PAP-I in terms of the molecular weight, subunit structure, affinity to the substrate, inhibitor profile and pH optimum. Immunoblot analysis using an antibody raised against recombinant rat PAP-I showed that rat PAP-I is present almost exclusively in the cytosolic fraction of the rat liver. Moreover, the hydrolyzing activity for L-pyroglutamyl p-nitroanilide in rat liver cytosolic fraction was completely inhibited by the antibody, strongly suggesting that this xenobiotic substrate is hydrolyzed solely by PAP-I. | lld:pubmed |
| pubmed-article:14600395 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14600395 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14600395 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14600395 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14600395 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14600395 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14600395 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14600395 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:14600395 | pubmed:issn | 0918-6158 | lld:pubmed |
| pubmed-article:14600395 | pubmed:author | pubmed-author:KnowE GEG | lld:pubmed |
| pubmed-article:14600395 | pubmed:author | pubmed-author:IkedaToshihik... | lld:pubmed |
| pubmed-article:14600395 | pubmed:author | pubmed-author:TokuiTaroT | lld:pubmed |
| pubmed-article:14600395 | pubmed:author | pubmed-author:YamadaMakikoM | lld:pubmed |
| pubmed-article:14600395 | pubmed:author | pubmed-author:WatanabeNobua... | lld:pubmed |
| pubmed-article:14600395 | pubmed:author | pubmed-author:KosakaToshiyu... | lld:pubmed |
| pubmed-article:14600395 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14600395 | pubmed:volume | 26 | lld:pubmed |
| pubmed-article:14600395 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14600395 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14600395 | pubmed:pagination | 1528-33 | lld:pubmed |
| pubmed-article:14600395 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:meshHeading | pubmed-meshheading:14600395... | lld:pubmed |
| pubmed-article:14600395 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14600395 | pubmed:articleTitle | Hydrolysis of synthetic substrate, L-pyroglutamyl p-nitroanilide is catalyzed solely by pyroglutamyl aminopeptidase I in rat liver cytosol. | lld:pubmed |
| pubmed-article:14600395 | pubmed:affiliation | Pharmacokinetics and Drug Delivery Research Laboratories, Sankyo Co., Ltd., Hiromachi, Tokyo 140-8710, Japan. koujia@shina.sankyo.co.jp | lld:pubmed |
| pubmed-article:14600395 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:290648 | entrezgene:pubmed | pubmed-article:14600395 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14600395 | lld:pubmed |
