scholarly journals Site of binding of mouse IgG2b to the Fc receptor on mouse macrophages.

1979 ◽  
Vol 150 (3) ◽  
pp. 721-726 ◽  
Author(s):  
B Diamond ◽  
B K Birshtein ◽  
M D Scharff
Keyword(s):  
Heavy Chain ◽  
Fc Receptors ◽  
Myeloma Cell ◽  
Fc Receptor ◽  
Heavy Chains ◽  
Mouse Macrophages ◽  
Mouse Myeloma Cell Line ◽  
Ch2 Domain ◽  
A Site ◽  
Mouse Myeloma

Three mouse immunoglobulins with altered heavy chains have been used to study the specificity of the mouse IgG2b Fc receptor on mouse macrophages. These immunoglobulins were synthesized by variant clones derived from the MPC 11, IgG2b-producing mouse myeloma cell line. One variant, whose Fc receptor. A second variant, which makes a short heavy chain lacking the CH3 domain, binds specifically to the IgG2b Fc receptor. The third variant makes a hybrid IgG2b-IgG2a heavy chain whose CH3 domain is enterely IgG2a-like and binds to both IgG2a and IgG2b Fc receptors. These data suggest that the binding of mouse IgG2b immunoglobulins to the mouse macrophage Fc receptor involves a site within the CH2 domain and indicate that immunoglobulins with altered heavy chains are a useful tool to probe Fc receptors.

scholarly journals Mouse myeloma cells that make short immunoglobulin heavy chains: pleiotropic effects on glycosylation and chain assembly.

1984 ◽  
Vol 98 (6) ◽  
pp. 2215-2221 ◽  
Author(s):  
A L Kenter ◽  
T Warren ◽  
D Shields ◽  
B K Birshtein
Keyword(s):  
Conformational Changes ◽  
Myeloma Cell ◽  
In Vitro Translation ◽  
Myeloma Cell Line ◽  
Present Evidence ◽  
Heavy Chains ◽  
Mouse Myeloma Cell ◽  
Mouse Myeloma Cell Line ◽  
Mouse Myeloma

Two variants in immunoglobulin heavy chain production, derived from the MPC 11 mouse myeloma cell line, make short heavy (H) chains with identical precise deletions of the CH3 domain. The CH3 domain is expressed in the H chain mRNA from both variants. Although in vitro translation of this mRNA produces one H chain species, deleted heavy chains are secreted as heavy-light (HL) and H2L2 moieties in contrast to MPC 11, which secretes only H2L2 . The heavy chains of HL apparently contain more carbohydrate (CHO+) than do the H chains of H2L2 , and inhibition of N-linked glycosylation results in the secretion of relatively more H2L2 . Here we present evidence suggesting that (a) the absence of the CH3 domain has led to conformational changes in these molecules, (b) these changes permit posttranslational glycosylation, and (c) unrestrained glycosylation can frequently yield unusual CHO+ structures that make complete assembly unlikely.

Nucleotide sequence of an unequal sister chromatid exchange site in a mouse myeloma cell line

1989 ◽  
Vol 9 (3) ◽  
pp. 1324-1326
Author(s):  
D R Katzenberg ◽  
S A Tilley ◽  
B K Birshtein
Keyword(s):  
Nucleotide Sequence ◽  
Cell Line ◽  
Sister Chromatid ◽  
Sister Chromatid Exchange ◽  
Present Report ◽  
Myeloma Cell ◽  
Myeloma Cell Line ◽  
Mouse Myeloma Cell ◽  
Mouse Myeloma Cell Line ◽  
Mouse Myeloma

The mouse myeloma cell line MPC 11 carries two C gamma 2a immunoglobulin heavy-chain genes on the expressed chromosome, a duplication shown to have occurred through unequal sister chromatid exchange (USCE). In the present report, we present the nucleotide sequence of the USCE joint and show that both breaks occurred within tracts of repeated TC dinucleotides. Additional TC dinucleotide tracts and two oligonucleotide segments (N sequences) were inserted at the USCE site.

Biochemical characterization of the cholesterol-dependent growth of the NS-1 mouse myeloma cell line

1986 ◽  
Vol 163 (1) ◽  
pp. 117-126 ◽  
Author(s):  
Jan-Kan Chen ◽  
Tetsuji Okamoto ◽  
J.Denry Sato ◽  
Gordon H. Sato ◽  
Don B. McClure
Keyword(s):  
Cell Line ◽  
Biochemical Characterization ◽  
Myeloma Cell ◽  
Myeloma Cell Line ◽  
Mouse Myeloma Cell ◽  
Mouse Myeloma Cell Line ◽  
Dependent Growth ◽  
Mouse Myeloma

scholarly journals Production and Characterization of Monoclonal Antibodies to Psittacine Beak and Feather Disease Virus

1992 ◽  
Vol 4 (1) ◽  
pp. 13-18 ◽  
Author(s):  
Branson W. Ritchie ◽  
Frank D. Niagro ◽  
Kenneth S. Latimer ◽  
W. L. Steffens ◽  
Denise Pesti ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Myeloma Cell ◽  
Enzyme Linked Immunosorbent Assay ◽  
Spleen Cells ◽  
Myeloma Cell Line ◽  
Elisa System ◽  
Mouse Myeloma Cell Line ◽  
Feather Disease Virus ◽  
Mouse Myeloma

Monoclonal antibodies specific for the virus that causes psittacine beak and feather disease (PBFD) were produced by fusing spleen cells from mice immunized with purified concentrated PBFD virus with mouse myeloma cell line Sp2/0. The resulting hybridomas were tested for reactivity against whole purified virus by an enzyme-linked immunosorbent assay (ELISA) system. Four clones, designated 15H8, 8E3, 11G12, and 2C3, were subcloned by limiting dilution. Isotyping indicated that clone 15H8 was secreting IgG, whereas the remaining clones secreted IgM. The secreted immunoglobulins were characterized by reactivity against purified PBFD virus using immunoblotting procedures, by immunohistochemical staining of virus-induced lesions in infected tissues, and by inhibition of PBFD virus agglutination of cockatoo erythrocytes. Antibodies secreted by clones 15H8 and 8E3 had the strongest activity against purified whole virus. Only immunoglobulin secreted by the clone 15H8 could be used to detect viral antigen in infected tissues. None of the monoclonal antibodies had hemagglutination-inhibition activity.

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