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001-es BibID:	BIBFORM002039
Első szerző:	Beck Zoltán (molekuláris biológus, mikrobiológus)
Cím:	Calcium modulation of monoclonal antibody binding to phosphatidylinositol phosphate / Zoltan Beck, Nicos Karasavvas, James Tong, Gary R. Matyas, Mangal Rao, Carl R. Alving
Dátum:	2007
Megjegyzések:	The binding characteristics of two monoclonal antibodies (mAb) to phosphatidylinositol-4-phosphate (PIP) were examined: a murine IgM mAb to PIP; and a human IgG mAb (4E10) that binds both to HIV-1 envelope protein and also to neutral and anionic phospholipids, including PIP. Binding of each mAb to pure PIP was inhibited by Ca2+ as determined by ELISA. When studied by surface plasmon resonance, liposomes containing PIP could be stripped (i.e., removed) by either Ca2+ or phosphorylated haptens after binding of the liposomes to the murine anti-PIP antibody attached to a BIAcore chip. In contrast, the binding of liposomal PIP to 4E10 was irreversible and could not be stripped. We therefore conclude that Ca2+ and phosphate can modulate the initial binding of both types of antibodies to PIP. However, 4E10 binds to liposomal PIP in a two-stage process involving first Ca2+-modulated binding to the PIP polar headgroup, followed by irreversible binding to liposomal hydrophobic groups.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban liposome calcium HIV-1 surface plasmon resonance phosphoinositide
Megjelenés:	Biochemical and Biophysical Research Communications. - 354 : 3 (2007), p. 747-751. -
További szerzők:	Karasavvas, Nicos Tong, James Matyas, Gary R. Rao, Mangala Alving, Carl R.
Internet cím:	elektronikus változat DOI elektronikus változat
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