Linked Life Data

16055397

Source:http://linkedlifedata.com/resource/pubmed/id/16055397

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2005-8-1
pubmed:abstractText
We found that N-unblocked nine p-nitroanilde derivatives of amino acids or peptides were hydrolyzed by the crude cell extracts of Streptococcus anginosus NCTC 10713. Then dipeptidyl peptidase IV was purified 323-fold by the procedures including ammonium sulfate concentration, anion exchange chromatography (twice), gel filtration (twice), hydrophobic interaction chromatography, and isoelectric focusing. The molecular weight was calculated as 84 kDa, and the isoelectric point was 4.9. The enzyme hydrolyzed mainly dipeptides containing proline residues at P1 position. It was strongly inhibited by serine enzyme inhibitors. General protease inhibitors, metal chelators, thiol alkylating agent, reducing agent, and several metal ions had no effect on the enzyme activity. Optimum pH for the activity was found at 7.0. The enzyme was mostly inactivated by heating at 50 degrees C for 15 min.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0949-2321
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
278-82
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Dipeptidyl peptidase IV of Streptococcus anginosus: purification and characterization.
pubmed:affiliation
Department of Oral Microbiology, Matsumoto Dental University, 1780 Hirooka-Gobara, Shiojiri-Shi, Nagano-Ken, 399-0781 Japan. fujimura@po.mdu.ac.jp
pubmed:publicationType
Journal Article