TY - JOUR
T1 - Biosynthesis and processing of murine T-cell antigen receptor
AU - McIntyre, Bradley W.
AU - Allison, James P.
N1 - Funding Information:
We wish to thank Judy Ing for help with preparation of the art work. This work was supported by grant CA 26321 from the National Institutes of Health. B. W. M. is the recipient of the J. S. Abercrombie predoctord fellowship.
PY - 1984/10
Y1 - 1984/10
N2 - The antigen-specific receptor of C6VL T-lymphoma cells is a disulfide-linked heterodimer composed of 39 kd α chain and a 41 kd β chain, both of which exhibit charge microheterogeneity. Pulse-chase labeling experiments indicate that epitopes reactive with the anti-receptor xenoantiserum #8177 were detectable by 2 min, while the clonotypic epitope reactive with monoclonal antibody 124-40 was not detectable until 10 min. Digestion with endoglycosidases H and F revealed that both subunits have at least three N-linked oligosaccharide side chains. The deglycosylated α and β subunits were 27 and 32 kd, respectively. These data suggest that the dimeric receptor is formed shortly after translation, followed by extensive glycosylation. Emergence of the C6VL clonotypic epitope, and perhaps the antigen binding site, may therefore be dependent on post-assembly events.
AB - The antigen-specific receptor of C6VL T-lymphoma cells is a disulfide-linked heterodimer composed of 39 kd α chain and a 41 kd β chain, both of which exhibit charge microheterogeneity. Pulse-chase labeling experiments indicate that epitopes reactive with the anti-receptor xenoantiserum #8177 were detectable by 2 min, while the clonotypic epitope reactive with monoclonal antibody 124-40 was not detectable until 10 min. Digestion with endoglycosidases H and F revealed that both subunits have at least three N-linked oligosaccharide side chains. The deglycosylated α and β subunits were 27 and 32 kd, respectively. These data suggest that the dimeric receptor is formed shortly after translation, followed by extensive glycosylation. Emergence of the C6VL clonotypic epitope, and perhaps the antigen binding site, may therefore be dependent on post-assembly events.
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U2 - 10.1016/0092-8674(84)90260-5
DO - 10.1016/0092-8674(84)90260-5
M3 - Article
C2 - 6488315
AN - SCOPUS:0021689953
SN - 0092-8674
VL - 38
SP - 659
EP - 665
JO - Cell
JF - Cell
IS - 3
ER -