Expression of a mouse-channel catfish chimeric IgM molecule in a mouse myeloma cell

1993 ◽  
Vol 30 (16) ◽  
pp. 1405-1417 ◽  
Author(s):  
Barry E. Ledford ◽  
Brad G. Magor ◽  
Darlene L. Middleton ◽  
Ronald L. Miller ◽  
Melanie R. Wilson ◽  
...  
Keyword(s):  
Channel Catfish ◽  
Myeloma Cell ◽  
Mouse Myeloma Cell ◽  
Mouse Myeloma

scholarly journals Differential Extraction of DNA Polymerase from the Nucleus of the Mouse Myeloma Cell

1979 ◽  
Vol 4 (4) ◽  
pp. 295-306 ◽  
Author(s):  
Akio Matsukage ◽  
Nobuyuki Nishioka ◽  
Miwako Nishizawa ◽  
Taijo Takahashi
Keyword(s):  
Dna Polymerase ◽  
Myeloma Cell ◽  
Differential Extraction ◽  
Mouse Myeloma Cell ◽  
Mouse Myeloma

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 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.

A soluble biotinyl-α-amanitin affinity probe for the isolation of RNA polymerase B

1986 ◽  
Vol 64 (9) ◽  
pp. 923-929 ◽  
Author(s):  
A. C. Vaisius ◽  
H. Faulstich
Keyword(s):  
Cell Culture ◽  
Rna Polymerase ◽  
Potent Inhibitor ◽  
Mammalian Cell Culture ◽  
Sodium Dodecyl ◽  
Myeloma Cell ◽  
Affinity Probe ◽  
Gel Beads ◽  
Mouse Myeloma Cell ◽  
Mouse Myeloma

Utilizing the 6′-hydroxyindole moiety of α-amanitin for substitution, biotinyl-α-amanitin has been synthesized to use as a soluble affinity probe for the isolation of RNA polymerase B from mammalian cell culture. The synthetic biotinyl-α-amanitin remains a potent inhibitor of RNA polymerase B having a Ki of 4.1 × 10−8 M as compared with a Ki of 5 × 10−9 M for natural α-amanitin. RNA polymerase B complexed with biotinyl-α-amanitin can be isolated on Bio-Gel P300 polyacrylamide gel beads to which avidin has been attached. RNA polymerase B may then be released from the complex by treatment with sodium dodecyl sulfate or by monochromatic irradiation at 314 nm which destroys the amatoxin moiety. We have used this affinity probe to analyze the subunit composition of RNA polymerase B from various mouse myeloma cell lines. We believe that the biotinyl-α-amanitin may be very useful for the isolation of factors which associate with RNA polymerase B; e.g., we have substantiated that actin can be associated with RNA polymerase.

Sign in / Sign up

Export Citation Format

Share Document