Linked Life Data

11843185

Source:http://linkedlifedata.com/resource/pubmed/id/11843185

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2002-2-14
pubmed:abstractText
We purified tripeptidyl peptidase I (TPP I) to homogeneity from a rat kidney lysosomal fraction and determined its physicochemical properties, including its molecular weight, substrate specificity and partial amino acid sequence. The molecular weight of the enzyme was calculated to be 280,000 and 290,000 by non-denaturing PAGE and gel filtration, respectively, and to be 43 000 and 46 000 on SDS-PAGE in the absence and presence of beta-ME, respectively. These findings suggest that the enzyme is composed of six identical subunits. The Km, Vmax, kcat and kcat/Km values of TPP I at optimal pH (pH 4.0) were 680 microM, 3.7 micromol x mg(-1) x min(-1), 33.1 s(-1) and 4.87 x 10(4) s(-1) x M(-1) for Ala-Ala-Phe-MCA, respectively. TPP I was significantly inhibited by PCMBS and HgCl2, and moderately by DFP. These findings also suggest that TPP I is an exotype serine peptidase that is regulated by SH reagent. TPP I released the tripeptide Arg-Val-Tyr from angiotensin III more rapidly than from Ala-Ala-Phe-MCA, and also released Gly-Asn-Leu from neuromedin B with the same velocity as from Ala-Ala-Phe-MCA. Angiotensin III and neuromedin B have recently been found to be good natural substrates for lysosomal TPP I. Furthermore, we determined the rat liver cDNA structure and deduced the amino acid sequence. The cDNA, designated as lambdaRTI-1, is composed of 2485 bp and encodes 563 amino acids in the coding region. By Northern blot analysis, the order for TPP I mRNA expression was kidney > or = liver > heart > brain > lung > spleen >> skeletal muscle and testis. In parallel experiments, the TPP I antigen was detected in various rat tissues by immunohistochemical staining.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1431-6730
pubmed:author
pubmed:issnType
Print
pubmed:volume
382
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1715-25
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11843185-Amino Acid Sequence, pubmed-meshheading:11843185-Aminopeptidases, pubmed-meshheading:11843185-Angiotensin III, pubmed-meshheading:11843185-Animals, pubmed-meshheading:11843185-Base Sequence, pubmed-meshheading:11843185-Blotting, Northern, pubmed-meshheading:11843185-Chromatography, Agarose, pubmed-meshheading:11843185-Chromatography, Gel, pubmed-meshheading:11843185-Cloning, Molecular, pubmed-meshheading:11843185-Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, pubmed-meshheading:11843185-Endopeptidases, pubmed-meshheading:11843185-Enzyme Inhibitors, pubmed-meshheading:11843185-Immunohistochemistry, pubmed-meshheading:11843185-Kidney, pubmed-meshheading:11843185-Mass Spectrometry, pubmed-meshheading:11843185-Molecular Sequence Data, pubmed-meshheading:11843185-Molecular Weight, pubmed-meshheading:11843185-Neurokinin B, pubmed-meshheading:11843185-Polymerase Chain Reaction, pubmed-meshheading:11843185-Rats, pubmed-meshheading:11843185-Rats, Wistar, pubmed-meshheading:11843185-Sequence Homology, Amino Acid, pubmed-meshheading:11843185-Serine Proteases, pubmed-meshheading:11843185-Substrate Specificity
pubmed:year
2001
pubmed:articleTitle
Rat tripeptidyl peptidase I: molecular cloning, functional expression, tissue localization and enzymatic characterization.
pubmed:affiliation
Department of Medical Biochemistry, Shiga University of Medical Science, Seta, Otsu, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't