Biochemical characterization of the human t6 antigen: A comparison between T6 and murine TL

Yuri Bushkin, Michael J. Chorney, Edson Diamante, Man Fu Shu Man Fu, Yi Wang Chang Yi Wang

Research output: Contribution to journalArticle

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Abstract

The human T6 antigen was studied by two monoclonal antibodies: OKT6 and Leu-6. A third monoclonal antibody, C56 (developed in our laboratory), was found to have similar properties to those of OKT6. On SDS-PAGE, all three antibodies precipitated a 48,000-12,000-dalton heterodimer. Two-dimensional gel electrophoresis and chymotryptic peptide map analysis revealed that these antibodies precipitated in identical 48,000-dalton heavy chain which was distinguishable from the HLA-A,B,C heavy chains. The single 12,000-dalton light chain precipitated with OKT6 antibody was shown to be distinct from β2-microglobulin by its pI. The two light chains precipitated with Leu-6 antibody were resolved by charge into β2-microglobulin and the more basic 12,000-dalton peptide identical to that precipitated with OKT6. In addition to β2-microglobulin, the latter component (presumably βt) was also found in the light-chain fraction precipitated from the thymocytes with a monoclonal antibody recognizing the framework of HLA-A,B,C heavy chains. Using chymotryptic peptide mapping, no polymorphism was detected among the heavy chains of the T6 antigen isolated from thymocytes of four individuals. All three monoclonal antibodies failed to precipitate murine TL from ASL1 leukemia cell lysates. Similarly, none of the six monoclonal and two conventional anti-TL antibodies reacted with T6. Although a high degree of homology was found by peptide map analysis among the TL molecules encoded by the Tlaa, Tlad and Tlae alleles, a comparison between their peptide maps and that of T6 revealed no similarity. Despite previous suggestions that T6 is homologous to murine TL, the present biochemical studies do not support this hypothesis.

Original languageEnglish (US)
Pages (from-to)821-829
Number of pages9
JournalMolecular Immunology
Volume21
Issue number10
DOIs
StatePublished - Oct 1984

Fingerprint

T Lymphocyte Differentiation Antigens
Monoclonal Antibodies
Peptides
HLA-A Antigens
HLA-B Antigens
Antibodies
Thymocytes
Light
Peptide Mapping
Electrophoresis, Gel, Two-Dimensional
Polyacrylamide Gel Electrophoresis
Anti-Idiotypic Antibodies
Leukemia
Alleles

All Science Journal Classification (ASJC) codes

  • Immunology
  • Molecular Biology

Cite this

Bushkin, Y., Chorney, M. J., Diamante, E., Shu Man Fu, M. F., & Chang Yi Wang, Y. W. (1984). Biochemical characterization of the human t6 antigen: A comparison between T6 and murine TL. Molecular Immunology, 21(10), 821-829. https://doi.org/10.1016/0161-5890(84)90135-4
Bushkin, Yuri ; Chorney, Michael J. ; Diamante, Edson ; Shu Man Fu, Man Fu ; Chang Yi Wang, Yi Wang. / Biochemical characterization of the human t6 antigen : A comparison between T6 and murine TL. In: Molecular Immunology. 1984 ; Vol. 21, No. 10. pp. 821-829.
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Bushkin, Y, Chorney, MJ, Diamante, E, Shu Man Fu, MF & Chang Yi Wang, YW 1984, 'Biochemical characterization of the human t6 antigen: A comparison between T6 and murine TL', Molecular Immunology, vol. 21, no. 10, pp. 821-829. https://doi.org/10.1016/0161-5890(84)90135-4

Biochemical characterization of the human t6 antigen : A comparison between T6 and murine TL. / Bushkin, Yuri; Chorney, Michael J.; Diamante, Edson; Shu Man Fu, Man Fu; Chang Yi Wang, Yi Wang.

In: Molecular Immunology, Vol. 21, No. 10, 10.1984, p. 821-829.

Research output: Contribution to journalArticle

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T1 - Biochemical characterization of the human t6 antigen

T2 - A comparison between T6 and murine TL

AU - Bushkin, Yuri

AU - Chorney, Michael J.

AU - Diamante, Edson

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AU - Chang Yi Wang, Yi Wang

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N2 - The human T6 antigen was studied by two monoclonal antibodies: OKT6 and Leu-6. A third monoclonal antibody, C56 (developed in our laboratory), was found to have similar properties to those of OKT6. On SDS-PAGE, all three antibodies precipitated a 48,000-12,000-dalton heterodimer. Two-dimensional gel electrophoresis and chymotryptic peptide map analysis revealed that these antibodies precipitated in identical 48,000-dalton heavy chain which was distinguishable from the HLA-A,B,C heavy chains. The single 12,000-dalton light chain precipitated with OKT6 antibody was shown to be distinct from β2-microglobulin by its pI. The two light chains precipitated with Leu-6 antibody were resolved by charge into β2-microglobulin and the more basic 12,000-dalton peptide identical to that precipitated with OKT6. In addition to β2-microglobulin, the latter component (presumably βt) was also found in the light-chain fraction precipitated from the thymocytes with a monoclonal antibody recognizing the framework of HLA-A,B,C heavy chains. Using chymotryptic peptide mapping, no polymorphism was detected among the heavy chains of the T6 antigen isolated from thymocytes of four individuals. All three monoclonal antibodies failed to precipitate murine TL from ASL1 leukemia cell lysates. Similarly, none of the six monoclonal and two conventional anti-TL antibodies reacted with T6. Although a high degree of homology was found by peptide map analysis among the TL molecules encoded by the Tlaa, Tlad and Tlae alleles, a comparison between their peptide maps and that of T6 revealed no similarity. Despite previous suggestions that T6 is homologous to murine TL, the present biochemical studies do not support this hypothesis.

AB - The human T6 antigen was studied by two monoclonal antibodies: OKT6 and Leu-6. A third monoclonal antibody, C56 (developed in our laboratory), was found to have similar properties to those of OKT6. On SDS-PAGE, all three antibodies precipitated a 48,000-12,000-dalton heterodimer. Two-dimensional gel electrophoresis and chymotryptic peptide map analysis revealed that these antibodies precipitated in identical 48,000-dalton heavy chain which was distinguishable from the HLA-A,B,C heavy chains. The single 12,000-dalton light chain precipitated with OKT6 antibody was shown to be distinct from β2-microglobulin by its pI. The two light chains precipitated with Leu-6 antibody were resolved by charge into β2-microglobulin and the more basic 12,000-dalton peptide identical to that precipitated with OKT6. In addition to β2-microglobulin, the latter component (presumably βt) was also found in the light-chain fraction precipitated from the thymocytes with a monoclonal antibody recognizing the framework of HLA-A,B,C heavy chains. Using chymotryptic peptide mapping, no polymorphism was detected among the heavy chains of the T6 antigen isolated from thymocytes of four individuals. All three monoclonal antibodies failed to precipitate murine TL from ASL1 leukemia cell lysates. Similarly, none of the six monoclonal and two conventional anti-TL antibodies reacted with T6. Although a high degree of homology was found by peptide map analysis among the TL molecules encoded by the Tlaa, Tlad and Tlae alleles, a comparison between their peptide maps and that of T6 revealed no similarity. Despite previous suggestions that T6 is homologous to murine TL, the present biochemical studies do not support this hypothesis.

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