Linked Life Data

3010997

Source:http://linkedlifedata.com/resource/pubmed/id/3010997

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1986-6-13
pubmed:abstractText
We have identified and isolated two new calcium-activated neutral hydrolases from human ventricular muscles. The one is an esterase, of which molecular weight was 300,000, required millimolar concentration of Ca2+, hydrolyzed Ac-Tyr-OEt X H2O, optiaml pH at 7.0. The other is an amidase, of which molecular weight was 70,000, also required millimolar concentration of Ca2+, hydrolyzed a synthetic substrate for chymotrypsin, Suc-Leu-Leu-Val-Tyr-MCA, with optimal pH at 7.2. Both enzymes did not degrade casein or contractile proteins (myosin, actin, troponin and tropomyosin). Their activities were not inhibited by exogenous protease inhibitors, leupeptin, antipain, monoiodoacetic acid and chymostatin, while the amidase activity was blocked by the endogenous inhibitor against calcium-activated neutral protease (CANP). Thus, their characters are different from chymotrypsin or CANP and they seems to be new hydrolases in the human heart.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
136
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
773-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Identification of two new calcium dependent hydrolases in the human heart.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't