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Immunity Commons

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Biochemistry, Biophysics, and Structural Biology

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Articles 121 - 122 of 122

Full-Text Articles in Immunity

Purification And Ligand Binding Of A Soluble Class I Mhc Molecule Consisting Of The First Three Domains Of H-2kd Fused To B2-Microglobulin Expressed In The Baculovirus/Insect Cell System, Francois Godeau, Immanuel F. Luescher, David M. Ojcius, Cecile Saucier, Estelle Mottez, Lucien Cabanie, Philippe Kourilsky Dec 1992

Purification And Ligand Binding Of A Soluble Class I Mhc Molecule Consisting Of The First Three Domains Of H-2kd Fused To B2-Microglobulin Expressed In The Baculovirus/Insect Cell System, Francois Godeau, Immanuel F. Luescher, David M. Ojcius, Cecile Saucier, Estelle Mottez, Lucien Cabanie, Philippe Kourilsky

All Dugoni School of Dentistry Faculty Articles

A recombinant baculovirus encoding a single-chain murine major histocompatibility complex class I molecule in which the first three domains of H-2Kd are fused to beta 2-microglobulin (beta 2-m) via a 15-amino acid linker has been isolated and used to infect lepidopteran cells. A soluble, 391-amino acid single-chain H-2Kd (SC-Kd) molecule of 48 kDa was synthesized and glycosylated in insect cells and could be purified in the absence of detergents by affinity chromatography using the anti-H-2Kd monoclonal antibody SF1.1.1.1. We tested the ability of SC-Kd to bind antigenic peptides using a direct binding assay based on photoaffinity labeling. The photoreactive derivative …


Cytolytic And Ion Channel Forming Properties Of The N-Terminus Of Lymphocyte Perforin, David M. Ojcius, Pedro M. Persechini, Li-Mou Zheng, Paulo C. Notaroberto, Sandro C. Adeodato, John Ding-E. Young Jun 1991

Cytolytic And Ion Channel Forming Properties Of The N-Terminus Of Lymphocyte Perforin, David M. Ojcius, Pedro M. Persechini, Li-Mou Zheng, Paulo C. Notaroberto, Sandro C. Adeodato, John Ding-E. Young

All Dugoni School of Dentistry Faculty Articles

Perforin lyses cells by binding to the target cell membrane, where it polymerizes into large nonspecific pores. It is shown here that the first 34 amino acids of the N-terminal region of either human or murine perforin are soluble in aqueous medium and spontaneously insert into membranes. The N-terminal peptides lyse liposomes and nucleated cells, and they form ion channels in planar bilayers, some of which are comparable to those previously described for perforin. The lytic activity of the N-terminal domains does not require calcium, is independent of the lipid headgroup composition, and can be inhibited by heparin. Tumor cells …