Structural characterization of H-2 antigens purified from mouse liver.
AUTOR(ES)
Henriksen, O
RESUMO
Papain solubilized H-2a histocompatibility antigens (H-2Kk plus H-2Dd) have been purified by a large-scale procedure that can routinely provide 2-3 mg of heavy chain from 1 kg of mouse liver. The heavy chains were homogeneous by sodium dodecyl sulfate electrophoresis. Disc gel electrophoresis resolved two protein bands that were identified as H-2Dd and H-2Kd by immune complex formation and autoradiography. Comparative amino acid composition and NH2-terminal sequence analyses of unfractionated H-2a, H-2Kk, and HLA suggested close structural relationships. However, the following observations suggest that papain cleaves these membrane bound antigens at different positions with respect to the COOH terminus: the molecular weight of the peptide portion of papain solubilized HLA is smaller than that of H-2 (30,000 versus 33,700); the COOH-terminal sequences are different; and, finally, papain-solubilized H-2 contains a free cysteine residue in addition to the two disulfide bridges that are present in both H-2 and HLA.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=392767Documentos Relacionados
- ASSOCIATION OF H-2 ANTIGENS WITH THE CELL MEMBRANE FRACTION OF MOUSE LIVER*
- Cell-free synthesis of mouse H-2 histocompatibility antigens.
- Biochemical characterization of alien H-2 antigens expressed on a methylcholanthrene-induced tumor.
- THE DISTRIBUTION IN THE TISSUES AND THE DEVELOPMENT OF H-2 ANTIGENS OF THE MOUSE*†
- Serological and Immunogenic Activity of Soluble Mouse Transplantation Antigens Controlled by the H-2 Locus
