Idiotypes of inulin-binding myeloma proteins localized to variable region light and heavy chains: genetic significance

نویسندگان

  • R Lieberman
  • M Vrana
  • W Humphrey
  • C C Chien
  • M Potter
چکیده

Idiotypes of inulin-binding myeloma proteins (InuBMP) were determined primarly by variable region light chains (VL) or by variable region heavy chains (VH) but needed both chains to be expressed. Recombinant molecules were used to show that individual idiotypes (IdI) of U61, E109, T957, and A4 InuBMP and cross-specific idiotypes (IdXB) of U61 were primarily determined by VL while cross-specific idiotype (IdXA) of A4 was determined mainly by VH. The assignment of genes controlling idiotypes to VH based on allotype linkage (e.g., IdXB) is dubious until the role of the L chain in determining that idiotype is assessed. IdXB has been shown to be a VL-VH marker which presumably is controlled by two unlinked genes. However IdXB can be used as a L chain marker in combinations of strains differing in their L chain genes but having the same permissive H chain genes. Conversely IdXB can be used as a H chain marker in strains having the same permissive L chain genes but differing in their H chain genes.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Structural Correlates of Cross-reactive and Individual Idiotypic Determinants on Murine Antibodies to A-(1 ~ 3) Dextran*

Since their first description over 20 years ago, idiotypes have been used extensively to study various aspects of the immune system (1, 2). Idiotypes, antigenic determinants associated with immunoglobulin-variable regions, have been found on VH and VL regions, or both (3-11), and have been localized to both antigen-binding and framework regions (12-17). Those idiotypes shared by immunoglobulins...

متن کامل

Determination of Superficial Clefts on Fragment of Antigen Binding in Human Immunoglobulin G by Computational Immunology

Background: Immunoglobulins (Igs) are protective glycoproteins specifically identify and eradicate microbes. Fragment of antigen binding (Fab) is a portion of antibody which binds to antigen and consists of one variable and one constant domain of one heavy and one light chain. Idiotypes, epitopes situated on Igs variable region, could be exploited to monitor and target malignant B cells and are...

متن کامل

EXPRESSION OF EQUIVALENT CLONOTYPES IN BALB/c AND A/J MICE AFTER IMMUNIZATION WITH PHOSPHORYLCHOLINE BY STUART RUDIKOFF AND J. LATHAM CLAFLIN*

A series of phosphorylcholine (PC) 1 binding myeloma proteins of BALB/c origin have been described and characterized by several laboratories (1-4). One group of these proteins, including among others T15, H8, and S107, has been shown to possess identical variable region antigenic determinants (idiotypes) (2, 5) as well as identical partial variable region light and heavy chain amino acid sequen...

متن کامل

Expression of an idiotype (Id-460) during in vivo anti-dinitrophenyl antibody responses. I. Mapping of genes for Id-460 expression to the variable region of immunoglobulin heavy-chain locus and to the variable region of immunoglobulin kappa-light-chain locus

The genetic contro of the expression of an idiotype (Id-460) associated with the 2,4-dinitrophenyl (DNP)-binding BALB/c myeloma protein MOPC 460 was studied using congenic strains of mice. It was shown that the expression of high levels of Id-460 during secondary in vivo anti-DNP-ovalbumin responses was determined by genes governing immunoglobulin heavy-chain variable and kappa-light chain vari...

متن کامل

Human and murine phosphorycholine-binding immunoglobulins: conserved subgroup and first hypervariable region of heavy chains.

The NH2-terminal 36 residues of the heavy chain and the NH2-terminal 40 residues of the light chain from a human Waldenström's IgM with binding activity for phosphorylcholine (phosphocholine) are compared with the published sequences of five mouse IgA myeloma proteins with the same activity. An extensive structural similarity; i.e., 3 amino acid interchanges within framework residues, and one i...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • The Journal of Experimental Medicine

دوره 146  شماره 

صفحات  -

تاریخ انتشار 1977