Purification and NH2-terminal amino acid sequencing of the beta subunit of a human T-cell antigen receptor.

To obtain information about the structural basis for T-cell antigen recognition, a T3-associated Ti receptor molecule was isolated from crude membranes of the REX human thymic tumor line and purified by affinity chromatography with an anti- clonotypic monoclonal antibody in conjunction with preparat...

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Main Authors: Acuto, O, Fabbi, M, Smart, J, Poole, C, Protentis, J, Royer, H, Schlossman, S, Reinherz, E
Format: Journal article
Language:English
Published: 1984
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author Acuto, O
Fabbi, M
Smart, J
Poole, C
Protentis, J
Royer, H
Schlossman, S
Reinherz, E
author_facet Acuto, O
Fabbi, M
Smart, J
Poole, C
Protentis, J
Royer, H
Schlossman, S
Reinherz, E
author_sort Acuto, O
collection OXFORD
description To obtain information about the structural basis for T-cell antigen recognition, a T3-associated Ti receptor molecule was isolated from crude membranes of the REX human thymic tumor line and purified by affinity chromatography with an anti- clonotypic monoclonal antibody in conjunction with preparative gel electrophoresis. NH2-terminal amino acid sequencing of the beta subunit unambiguously identified the amino acids in positions 2-12. Comparative protein sequence analysis by computer search demonstrated that this Ti beta sequence bore weak, but definite, homology to the first framework of the variable region of human lambda light chain. Anti-sera to a synthetic peptide corresponding to positions 2-11 precipitated the denatured Ti beta subunit from REX, thus confirming the above sequence. This information suggests that the Ti beta subunit is distantly related to human immunoglobulin lambda light chain and, moreover, should be of use in the molecular cloning of the Ti beta gene.
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spelling oxford-uuid:071249c6-f709-4eaa-9e47-e01a43277c162022-03-26T09:05:45ZPurification and NH2-terminal amino acid sequencing of the beta subunit of a human T-cell antigen receptor.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:071249c6-f709-4eaa-9e47-e01a43277c16EnglishSymplectic Elements at Oxford1984Acuto, OFabbi, MSmart, JPoole, CProtentis, JRoyer, HSchlossman, SReinherz, ETo obtain information about the structural basis for T-cell antigen recognition, a T3-associated Ti receptor molecule was isolated from crude membranes of the REX human thymic tumor line and purified by affinity chromatography with an anti- clonotypic monoclonal antibody in conjunction with preparative gel electrophoresis. NH2-terminal amino acid sequencing of the beta subunit unambiguously identified the amino acids in positions 2-12. Comparative protein sequence analysis by computer search demonstrated that this Ti beta sequence bore weak, but definite, homology to the first framework of the variable region of human lambda light chain. Anti-sera to a synthetic peptide corresponding to positions 2-11 precipitated the denatured Ti beta subunit from REX, thus confirming the above sequence. This information suggests that the Ti beta subunit is distantly related to human immunoglobulin lambda light chain and, moreover, should be of use in the molecular cloning of the Ti beta gene.
spellingShingle Acuto, O
Fabbi, M
Smart, J
Poole, C
Protentis, J
Royer, H
Schlossman, S
Reinherz, E
Purification and NH2-terminal amino acid sequencing of the beta subunit of a human T-cell antigen receptor.
title Purification and NH2-terminal amino acid sequencing of the beta subunit of a human T-cell antigen receptor.
title_full Purification and NH2-terminal amino acid sequencing of the beta subunit of a human T-cell antigen receptor.
title_fullStr Purification and NH2-terminal amino acid sequencing of the beta subunit of a human T-cell antigen receptor.
title_full_unstemmed Purification and NH2-terminal amino acid sequencing of the beta subunit of a human T-cell antigen receptor.
title_short Purification and NH2-terminal amino acid sequencing of the beta subunit of a human T-cell antigen receptor.
title_sort purification and nh2 terminal amino acid sequencing of the beta subunit of a human t cell antigen receptor
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