Biochemical characterization of a P43,12 complex: Comparison with human and murine class I molecules

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

Research output: Contribution to journalArticle

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Abstract

A monoclonal antibody designated as C21 reacting with a p43,12 complex was developed against human thymocytes. It stained predominantly the early hematopoietic cells of the lymphoid lineage and also thymocytes, peripheral B-cells and activated T- and B-cells similarly to OKT10. The heavy chain of this antigen was a glycoprotein of M, 43,000 (p43). Sequential immunoprecipitation with C21 and OKT10 antibodies indicated that they both reacted with an identical heavy-chain molecule. This observation was further documented by two-dimensional analysis. Monoclonal antibody C21 was used to probe a p43,12 complex further. Structural polymorphism of the p43 heavy chain isolated from T- and B-cells of different individuals was not detected by chymotryptic peptide mappIng, although molecules from these cell types possessed a different charge on two-dimensional gels. An unusual observation was made regarding this complex on MOLT4 cells. The light chain co-precipitated from these cells was 12,000 daltons and had a pI distinct from that of β2-microglobulin but similar to the pI of the βt molecule. Comparison between chymotryptic peptide maps of the p43 heavy chain and those of the human and murine class I molecules such as HLA, T6, H-2K, Qa-2 and TL revealed no apparent homology. We have shown, however, that the peptide backbone of p43, as studied by both tunicamycin treatment of cells and endoglycosidase F digestion of immunoprecipitates, was identical in size to that of murine Qa-1. These results suggest that the p43 antigen may be homologous to murine Qa-1 or another class I antigen encoded in the murine TL:Qa region.

Original languageEnglish (US)
Pages (from-to)695-703
Number of pages9
JournalMolecular Immunology
Volume22
Issue number6
DOIs
StatePublished - Jun 1985

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B-Lymphocytes
Thymocytes
Monoclonal Antibodies
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
Antigens
Tunicamycin
Histocompatibility Antigens Class I
Peptides
Peptide Mapping
Cell Lineage
Immunoprecipitation
Digestion
Glycoproteins
Gels
Observation
Light
Antibodies

All Science Journal Classification (ASJC) codes

  • Immunology
  • Molecular Biology

Cite this

Bushkin, Y., Chorney, M. J., Diamante, E., Lane, C., Shu Man Fu, M. F., & Chang Yi Wang, Y. W. (1985). Biochemical characterization of a P43,12 complex: Comparison with human and murine class I molecules. Molecular Immunology, 22(6), 695-703. https://doi.org/10.1016/0161-5890(85)90100-2
Bushkin, Yuri ; Chorney, Michael J. ; Diamante, Edson ; Lane, Caryl ; Shu Man Fu, Man Fu ; Chang Yi Wang, Yi Wang. / Biochemical characterization of a P43,12 complex : Comparison with human and murine class I molecules. In: Molecular Immunology. 1985 ; Vol. 22, No. 6. pp. 695-703.
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abstract = "A monoclonal antibody designated as C21 reacting with a p43,12 complex was developed against human thymocytes. It stained predominantly the early hematopoietic cells of the lymphoid lineage and also thymocytes, peripheral B-cells and activated T- and B-cells similarly to OKT10. The heavy chain of this antigen was a glycoprotein of M, 43,000 (p43). Sequential immunoprecipitation with C21 and OKT10 antibodies indicated that they both reacted with an identical heavy-chain molecule. This observation was further documented by two-dimensional analysis. Monoclonal antibody C21 was used to probe a p43,12 complex further. Structural polymorphism of the p43 heavy chain isolated from T- and B-cells of different individuals was not detected by chymotryptic peptide mappIng, although molecules from these cell types possessed a different charge on two-dimensional gels. An unusual observation was made regarding this complex on MOLT4 cells. The light chain co-precipitated from these cells was 12,000 daltons and had a pI distinct from that of β2-microglobulin but similar to the pI of the βt molecule. Comparison between chymotryptic peptide maps of the p43 heavy chain and those of the human and murine class I molecules such as HLA, T6, H-2K, Qa-2 and TL revealed no apparent homology. We have shown, however, that the peptide backbone of p43, as studied by both tunicamycin treatment of cells and endoglycosidase F digestion of immunoprecipitates, was identical in size to that of murine Qa-1. These results suggest that the p43 antigen may be homologous to murine Qa-1 or another class I antigen encoded in the murine TL:Qa region.",
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Bushkin, Y, Chorney, MJ, Diamante, E, Lane, C, Shu Man Fu, MF & Chang Yi Wang, YW 1985, 'Biochemical characterization of a P43,12 complex: Comparison with human and murine class I molecules', Molecular Immunology, vol. 22, no. 6, pp. 695-703. https://doi.org/10.1016/0161-5890(85)90100-2

Biochemical characterization of a P43,12 complex : Comparison with human and murine class I molecules. / Bushkin, Yuri; Chorney, Michael J.; Diamante, Edson; Lane, Caryl; Shu Man Fu, Man Fu; Chang Yi Wang, Yi Wang.

In: Molecular Immunology, Vol. 22, No. 6, 06.1985, p. 695-703.

Research output: Contribution to journalArticle

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T1 - Biochemical characterization of a P43,12 complex

T2 - Comparison with human and murine class I molecules

AU - Bushkin, Yuri

AU - Chorney, Michael J.

AU - Diamante, Edson

AU - Lane, Caryl

AU - Shu Man Fu, Man Fu

AU - Chang Yi Wang, Yi Wang

PY - 1985/6

Y1 - 1985/6

N2 - A monoclonal antibody designated as C21 reacting with a p43,12 complex was developed against human thymocytes. It stained predominantly the early hematopoietic cells of the lymphoid lineage and also thymocytes, peripheral B-cells and activated T- and B-cells similarly to OKT10. The heavy chain of this antigen was a glycoprotein of M, 43,000 (p43). Sequential immunoprecipitation with C21 and OKT10 antibodies indicated that they both reacted with an identical heavy-chain molecule. This observation was further documented by two-dimensional analysis. Monoclonal antibody C21 was used to probe a p43,12 complex further. Structural polymorphism of the p43 heavy chain isolated from T- and B-cells of different individuals was not detected by chymotryptic peptide mappIng, although molecules from these cell types possessed a different charge on two-dimensional gels. An unusual observation was made regarding this complex on MOLT4 cells. The light chain co-precipitated from these cells was 12,000 daltons and had a pI distinct from that of β2-microglobulin but similar to the pI of the βt molecule. Comparison between chymotryptic peptide maps of the p43 heavy chain and those of the human and murine class I molecules such as HLA, T6, H-2K, Qa-2 and TL revealed no apparent homology. We have shown, however, that the peptide backbone of p43, as studied by both tunicamycin treatment of cells and endoglycosidase F digestion of immunoprecipitates, was identical in size to that of murine Qa-1. These results suggest that the p43 antigen may be homologous to murine Qa-1 or another class I antigen encoded in the murine TL:Qa region.

AB - A monoclonal antibody designated as C21 reacting with a p43,12 complex was developed against human thymocytes. It stained predominantly the early hematopoietic cells of the lymphoid lineage and also thymocytes, peripheral B-cells and activated T- and B-cells similarly to OKT10. The heavy chain of this antigen was a glycoprotein of M, 43,000 (p43). Sequential immunoprecipitation with C21 and OKT10 antibodies indicated that they both reacted with an identical heavy-chain molecule. This observation was further documented by two-dimensional analysis. Monoclonal antibody C21 was used to probe a p43,12 complex further. Structural polymorphism of the p43 heavy chain isolated from T- and B-cells of different individuals was not detected by chymotryptic peptide mappIng, although molecules from these cell types possessed a different charge on two-dimensional gels. An unusual observation was made regarding this complex on MOLT4 cells. The light chain co-precipitated from these cells was 12,000 daltons and had a pI distinct from that of β2-microglobulin but similar to the pI of the βt molecule. Comparison between chymotryptic peptide maps of the p43 heavy chain and those of the human and murine class I molecules such as HLA, T6, H-2K, Qa-2 and TL revealed no apparent homology. We have shown, however, that the peptide backbone of p43, as studied by both tunicamycin treatment of cells and endoglycosidase F digestion of immunoprecipitates, was identical in size to that of murine Qa-1. These results suggest that the p43 antigen may be homologous to murine Qa-1 or another class I antigen encoded in the murine TL:Qa region.

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