Linked Life Data

6853510

Source:http://linkedlifedata.com/resource/pubmed/id/6853510

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1983-7-15
pubmed:abstractText
The amino acid sequence variation among seven lactate dehydrogenase isozymes from dogfish muscle, chicken muscle and heart, pig muscle and heart, and mouse and rat testes were compared with respect to the whole lactate dehydrogenase polypeptide chain as well as their four functional domains. The coenzyme-binding domain is more conserved than the substrate-binding domain. The sequence of the loop and helix alpha D region of testicular LDH-C4 isozymes is very different from those of somatic LDH-A4 and LDH-B4 isozymes, while the NH2-terminal arm is extremely variable. The most parsimonious phylogenetic tree among these seven vertebrate lactate dehydrogenase sequences clearly indicates that the LDH-A4 and LDH-B4 isozymes are more closely related to each other than either to the LDH-C4 isozymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
258
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7029-32
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Evolutionary relationships of vertebrate lactate dehydrogenase isozymes A4 (muscle), B4 (heart), and C4 (testis).
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S.