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383


Structural comparison of murine Ia antigens determined by the I-A and I-E subregions

Cullen SE; Kindle CS; Littman DR
PMID: 448079
ISSN: 0022-1767
CID: 15193

Insertion of Ia and H-2 alloantigens into model membranes

Littman DR; Cullen SE; Schwartz BD
The study of immune phenomena dependent on the major histocompatibility complex (MHC) would be greatly simplified by the use of MHC antigen-containing liposomes in various functional systems. Towards this end, we have constructed unilamellar phosphatidylcholine liposomes containing H-2 and Ia antigens. These molecules were not simply trapped within the aqueous compartment of the liposome as assessed by their accessibility to papain digestion. They were shown to be integrally inserted in the liposome bilayer because they could not be dissociated from the liposome with high salt and EDTA concentrations but could be solubilized by detergent. A sensitive radioimmunoassay showed that the Ia molecules were antigenically active in the liposome environment. Both Ia and H-2 antigens could be immunoprecipitated from detergent-solubilized liposomes. By comparing liposome-associated Ia activity in the presence and absence of detergent and by showing accessibility of the Ia antigens to papain, it was concluded that the majority of Ia antigens were exposed on the external surface of the liposome. These results suggest that the orientation of MHC antigens in liposomes closely parallels their natural orientation in the cell membrane
PMCID:383087
PMID: 284415
ISSN: 0027-8424
CID: 15194

Properties of the depolymerization products of microtubules from mammalian brain

Weingarten MD; Suter MM; Littman DR; Kirschner MW
PMID: 4457112
ISSN: 0006-2960
CID: 15195