Linked Life Data

15202499

Source:http://linkedlifedata.com/resource/pubmed/id/15202499

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-6-18
pubmed:abstractText
Muscle-type LDH (LDH-m4) activity is critical for efficient anaerobic glycolysis. The results here show that rabbit LDH-M4 is inhibited by concentrations of ascorbate normally found in tissues. Aldolase and muscle G-actin were found to protect and to reverse inhibitions of LDH-m4 by ascorbate. G-actins showed some species specificity. Myosin, tropomyosin and troponin from rabbit muscle and muscle proteins from other animal sources had no affect on the inhibitions by ascorbate. The substrate inhibition of LDH-m4 by pyruvate is partially relieved by the presence of aldolase and lowers the Km without affecting the Vm. G-actin under similar conditions has no affect. It is believed that these studies reflect some of the resting properties of glycolytic enzymes that bind and unbind to contractile elements. It is proposed that ascorbate facilitates the storage of glycogen in muscle at rest by inhibiting glycolysis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1475-6366
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
91-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Aldolase and actin protect rabbit muscle lactate dehydrogenase from ascorbate inhibition.
pubmed:affiliation
Department of Biology, University of California 0690, San Diego, La Jolla, CA 92093-0690, USA. prussell@ucsd.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.