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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1990-9-10
|
| pubmed:abstractText |
High performance anion-exchange chromatography was used to separate two carnosine-hydrolysing dipeptidases from hog kidney. Both enzymes (peaks I and II) were cytosolic and were activated and stabilized by Mn2+ and dithiothreitol. Peak I had a narrow specificity when assayed without added metal ions, but a broad specificity in the presence of Mn2+ or Co2+. Peak II was inactive unless both Mn2+ and dithiothreitol were present. Bestatin and leucine inhibited peak II, but not peak I. Peak I had a Km of 0.4 mM carnosine, a pI of 5.5 and a Mr of 57,000. Peak II had a Km of 5 mM carnosine, a pI of 5.0 and a Mr of 70,000. Hog and rat brain and liver carnosinase activity was completely inhibited by bestatin, indicating that these organs contained peak II, with little or no peak I enzyme. Hog kidney peak I contained the classical carnosinase of Hanson and Smith, who first described this enzyme. It also contained activity against homocarnosine ("homocarnosinase") and showed "manganese-independent carnosinase" activity. These three activities could not be separated using 8 different chromatographic procedures; it was concluded that they are attributable to one enzyme. It is recommended that the name carnosinase be retained for this enzyme and the names "homocarnosinase" and "manganese-independent carnosinase" be withdrawn. The properties of hog kidney peak II closely resembled those of human tissue carnosinase (also known as prolinase, a non-specific dipeptidase), mouse "manganese-dependent carnosinase" and a rat brain enzyme termed "beta-Ala-Arg hydrolase". Since these terms appear to represent closely related enzymes with broad specificity, the recommended name for each is "non-specific cytosolic dipeptidase".
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anions,
http://linkedlifedata.com/resource/pubmed/chemical/Carnosine,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Dithiothreitol,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/aminoacyl-histidine dipeptidase
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0177-3593
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
371
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
433-40
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2378680-Amino Acid Sequence,
pubmed-meshheading:2378680-Animals,
pubmed-meshheading:2378680-Anions,
pubmed-meshheading:2378680-Carnosine,
pubmed-meshheading:2378680-Chromatography, Ion Exchange,
pubmed-meshheading:2378680-Cytosol,
pubmed-meshheading:2378680-Dipeptidases,
pubmed-meshheading:2378680-Dithiothreitol,
pubmed-meshheading:2378680-Dose-Response Relationship, Drug,
pubmed-meshheading:2378680-Enzyme Activation,
pubmed-meshheading:2378680-Enzyme Stability,
pubmed-meshheading:2378680-Humans,
pubmed-meshheading:2378680-Hydrogen-Ion Concentration,
pubmed-meshheading:2378680-Hydrolysis,
pubmed-meshheading:2378680-Isoelectric Point,
pubmed-meshheading:2378680-Kidney,
pubmed-meshheading:2378680-Manganese,
pubmed-meshheading:2378680-Mice,
pubmed-meshheading:2378680-Molecular Sequence Data,
pubmed-meshheading:2378680-Molecular Weight,
pubmed-meshheading:2378680-Rats,
pubmed-meshheading:2378680-Substrate Specificity,
pubmed-meshheading:2378680-Tissue Distribution
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
Separation and characterization of two carnosine-splitting cytosolic dipeptidases from hog kidney (carnosinase and non-specific dipeptidase).
|
| pubmed:affiliation |
Department of Pharmacology, School of Medicine, University of Hawaii.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|