Linked Life Data

2141325

Source:http://linkedlifedata.com/resource/pubmed/id/2141325

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-7-20
pubmed:abstractText
Rabbits immunized with dinitrophenylated calmodulin produced monospecific antibody against CaM. Using the purified antibody, enzyme-linked immunosorbent assays (ELISAs) were carried out for calmodulin (CaM). The immunological heterogeneity of human and bovine CaMs from erythrocytes was investigated by means of indirect and inhibition ELISAs. The cross-reactivity between the two CaMs was found to be 50% in the indirect ELISA. An eight times higher concentration of human CaM was necessary to produce 30% inhibition in an inhibition assay. The effect of anti-bovine CaM on the stimulation of the red cell membrane calcium pump by human and bovine CaM has also been studied. We have found that (a) the human and bovine CaMs showed indistinguishable activator activities; (b) the antibody partially inhibited the stimulating effects of CaMs; (c) the inhibition was much less effective in the case of stimulation by human CaM. These results suggest that there is a difference in the reactivity of the anti-bovine CaM antibody with bovine and human CaMs. This difference can be attributed to a slight deviation in the antibody binding structure of the two mammalian CaMs in or near the antigenic site of the CaMs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0165-2478
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
87-92
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Structurally distinct mammalian calmodulins.
pubmed:affiliation
Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't