Mouse invariant chain γ exhibits structural homology to both polymorphic subunits of the α,β‐core complex of I‐Ak antigens

FEBS Letters

Zecher, Reinhard¹  Stenger, Elisabeth¹  Reske, Konrad¹ 

[1] Institut für Immunologie der Joh. Gutenberg-Universität, Obere Zahlbacher Str. 67, D-6500 Mainz, FRG

关键词: MHC class II antigen;    Spleen lymphocyte;    Radiolabeling;    2D O'Farrell gel;    Electroblotting;    Comparative peptide analysis;    MHC;    major histocompatibility complex;    TPCK;    N-tosylphenylalanine chloromethyl ketone;    DTT;    dithiothreitol;    SDS—PAGE;    sodium dodecyl sulfate—polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(83)80436-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The 3 major constituents of the I-A^k subregion-associated complex α, β and γ were obtained from splenocytes in homogeneous form by differential isolation methods. α, β and γ were compared on the primary structural level by enzymatic fragmentation procedures and tryptic peptide map analysis of radiolabeled proteins. The data indicate that the invariant chain γ exhibits extensive structural homology to the polymorphic β-light and the α-heavy chain. Thus, although not being encoded within the MHC γ appears to belong structurally to the MHC-encoded class II proteins.

【 授权许可】

Unknown