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The major histocompatibility complex of rhesus monkeys. VIII. Isolation and partial characterization of SD antigens.

Authors
  • Giphart, M J
  • Tank, B
  • Bruning, J W
  • Balner, H
Type
Published Article
Journal
Transplantation Journal
Publisher
Ovid Technologies (Wolters Kluwer) - Lippincott Williams & Wilkins
Publication Date
March 1978
Volume
25
Issue
3
Pages
131–135
Identifiers
PMID: 417437
Source
Medline
License
Unknown

Abstract

The structure and chemical nature of the serologically defined (SD) antigens coded by the major histocompatibility complex (RhLA) of rhesus monkeys was studied. The use of specific anti-SD sera allowed the selective isolation of the corresponding antigens from crude antigen preparations. These were obtained by detergent solubilization after incorporation of 3H, 35S, and 14C amino acids in lymphocytes or mitogen-stimulated lymphoblasts. The results indicate that the SD antigens are of proteinaceous nature and are composed of two polypeptide chains with molecular weights of 44,000 and 12,000, the latter being beta 2-microglobulin. No differences in molecular size and subunit composition were detected between antigens of both segregant series. The results are discussed in relation to similar data available for the analogous human and murine histocompatibility antigens.

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