Biochemical characterization of Ia antigens. I. Characterization of the 31K polypeptide associated with I-A subregion Ia antigens

J. P. Moosic, A. Nilson, Peter J. Haemmerling, D. J. McKean

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Abstract

Procedures are presented for the preparative isolation of murine Ia antigens directly from splenocyte detergent extracts with monoclonal immunoadsorbents. Utilizing these procedures, three Ia (I-A subregion) polypeptides (α, 31K, β) were isolated and their m.w. and pI values characterized. Evidence is presented that indicates that: 1) the 31K polypeptide probably does not associate with the Ia α and β chain complex during the Ia isolation procedure; 2) the 31K polypeptide is not tightly bound to the α/β Ia complex and can be selectively removed by freezing and thawing and by washing the Ia-immunoadsorbent with buffers containing pyrrolidinone (a polar solvent); and (3) unlike the α and β chains, the 31K polypeptide is not intrinsically radiolabeled with 3H fucose and 3H glucosamine, indicating that the 31K polypeptide either contains a carbohydrate structure that is differemt from that of the α and β chains or it is not a glycopeptide. These data suggest that although Ia antigens are probably comprised of three polypeptides in the intact cell, only two (α and β) are required to maintain alloantigenic determinants.

Original languageEnglish (US)
Pages (from-to)1463-1469
Number of pages7
JournalJournal of Immunology
Volume125
Issue number4
StatePublished - Jan 1 1980

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Histocompatibility Antigens Class II
Peptides
Immunosorbents
Pyrrolidinones
Fucose
Glycopeptides
Glucosamine
Detergents
Freezing
Buffers
Carbohydrates

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Cite this

Biochemical characterization of Ia antigens. I. Characterization of the 31K polypeptide associated with I-A subregion Ia antigens. / Moosic, J. P.; Nilson, A.; Haemmerling, Peter J.; McKean, D. J.

In: Journal of Immunology, Vol. 125, No. 4, 01.01.1980, p. 1463-1469.

Research output: Contribution to journalArticle

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AB - Procedures are presented for the preparative isolation of murine Ia antigens directly from splenocyte detergent extracts with monoclonal immunoadsorbents. Utilizing these procedures, three Ia (I-A subregion) polypeptides (α, 31K, β) were isolated and their m.w. and pI values characterized. Evidence is presented that indicates that: 1) the 31K polypeptide probably does not associate with the Ia α and β chain complex during the Ia isolation procedure; 2) the 31K polypeptide is not tightly bound to the α/β Ia complex and can be selectively removed by freezing and thawing and by washing the Ia-immunoadsorbent with buffers containing pyrrolidinone (a polar solvent); and (3) unlike the α and β chains, the 31K polypeptide is not intrinsically radiolabeled with 3H fucose and 3H glucosamine, indicating that the 31K polypeptide either contains a carbohydrate structure that is differemt from that of the α and β chains or it is not a glycopeptide. These data suggest that although Ia antigens are probably comprised of three polypeptides in the intact cell, only two (α and β) are required to maintain alloantigenic determinants.

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