By Solheim J.C.
Well-recognized and leading edge experimentalists element their state-of-the-art tools for learning the antigen processing and presentation. Drawing on services from biochemistry, phone biology, and immunology, they describe step by step tools designed to question how MHC-binding peptides are generated, to check how peptides are brought to MHC molecules, to investigate MHC peptide-binding styles, and to assay the T-cell reaction to the MHC/peptide complicated. Emphasis is given these technical steps severe for experimental good fortune which are frequently passed over from tools released within the fundamental literature. Eminently obtainable and state of the art, Antigen Processing and Presentation Protocols presents either new and skilled investigators with hugely useful instruments that might expand the questions that may be requested, and successfully be responded, pertaining to antigen processing/presentation.
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McCormack, T. , Melandri, F. , et al. (1997) Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells. J. Biol. Chem. 272, 182–188. Peptides and MHC-I in Ag Presentation 33 3 Tracing the Route Taken by Peptides and Major Histocompatibility Complex Class I Molecules in Presentation of Exogenous Antigens Christopher C. Norbury 1. Introduction Since the discovery of cross priming by Bevan (1) nearly thirty years ago, a large amount of work has focused on defining the mechanisms that account for this in vivo phenomenon.
Int. J. Biochem. Cell Biol. 29, 611–622. 13. Koohmaraie, M. (1992) Ovine skeletal muscle multicatalytic proteinase complex (proteasome): purification, characterization, and comparison of its effects on myofibrils with µ-calpains. J. Anim. Sci. 70, 3697–3708. 14. Mykles, D. L. (1989) Purification and characterization of a multicatalytic proteinase from crustacean muscle: comparison of latent and heat-activated forms. Arch. Biochem. Biophys. 274, 216–228. 15. , and Nakagawa, H. (1992) Purification and initial characterization of the proteasome from the higher plant Spinacia oleracea.
Wash filters with 10% TFA (w/v), dry, and place in appropriate vials with biodegradable scintillation fluid, and count the filters in a β-counter. 8. Adjust the volumes of each sample used for immunoprecipitation, so that each sample contains the same amount of incorporated 35S-Met. Prepare two aliquots with each sample. 9. To one of the aliquots, add a class I-binding synthetic peptide (final concentration 5 µg/mL). Incubate all the samples, with or without peptide, at 37°C for 2 h, then incubate the extracts on ice.