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pubmed-article:8806598pubmed:abstractTextBoth 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.lld:pubmed
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pubmed-article:8806598pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:8806598pubmed:articleTitleEvidence of a laminin binding protein on the surface of Leishmania donovani.lld:pubmed
pubmed-article:8806598pubmed:affiliationMolecular Cell Biology Division, Indian Institute of Chemical Biology, Calcutta, India.lld:pubmed
pubmed-article:8806598pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8806598pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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