Linked Life Data

8806598

Source:http://linkedlifedata.com/resource/pubmed/id/8806598

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-10-22
pubmed:abstractText
Both the promastigote and amastigote forms of the intracellular parasite, Leishmania donovani bind the basement membrane glycoprotein laminin with high affinity (Kd = 3.56 x 10(-9) M and 3.98 x 10(-9) M respectively) with approximately 9000 and approximately 800 sites per cell. Bound laminin was identified by direct autoradiography and the binding protein through analysis of the parasite extract by SDS-PAGE and immunoblotting. A major component of 67 kDa was detected. The same protein was obtained when parasite outer membrane proteins were adsorbed to laminin-sepharose affinity matrix and subsequently eluted with SDS. The binding affinity of the isolated receptor was similar to that of the whole cells. Such a receptor isolated in Leishmania for the first time, may function as one of the bridging molecules for extracellular matrix recognition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
226
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
101-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Evidence of a laminin binding protein on the surface of Leishmania donovani.
pubmed:affiliation
Molecular Cell Biology Division, Indian Institute of Chemical Biology, Calcutta, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't