scholarly journals César Milstein CH. 8 October 1927 – 24 March 2002

2005 ◽  
Vol 51 ◽  
pp. 267-289 ◽  
Author(s):  
Michael S. Neuberger ◽  
Brigitte A. Askonas

César Milstein was a scientist of the greatest distinction who made seminal contributions to our knowledge and understanding of antibodies. He advanced our knowledge of their structure, their expression, the generation of antibody diversity and the maturation of antibody affinity that occurs during the course of an immune response. Most spectacular was his discovery (jointly with Georges Köhler) of a method for obtaining monoclonal antibodies of predefined antigen specificity by fusing a continuously growing mouse myeloma cell line with a normal lymphocyte making monospecific antibody. For this, Milstein and Köhler received the Nobel Prize for Physiology or Medicine in 1984. Although this discovery was the product of a purely academic project, its impact on medicine and technology as well as in fundamental research has been enormous, opening new avenues in diagnostics and therapy. César Milstein remained an enthusiastic, creative and passionate scientist throughout his life.

1989 ◽  
Vol 9 (3) ◽  
pp. 1324-1326
Author(s):  
D R Katzenberg ◽  
S A Tilley ◽  
B K Birshtein

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.


1986 ◽  
Vol 163 (1) ◽  
pp. 117-126 ◽  
Author(s):  
Jan-Kan Chen ◽  
Tetsuji Okamoto ◽  
J.Denry Sato ◽  
Gordon H. Sato ◽  
Don B. McClure

1984 ◽  
Vol 98 (6) ◽  
pp. 2215-2221 ◽  
Author(s):  
A L Kenter ◽  
T Warren ◽  
D Shields ◽  
B K Birshtein

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.


2003 ◽  
Vol 22 (5) ◽  
pp. 321-327 ◽  
Author(s):  
Marina B. Melixetian ◽  
Maria A. Pavlenko ◽  
Elena V. Beriozkina ◽  
Zoya V. Kovaleva ◽  
Elena A. Sorokina ◽  
...  

1989 ◽  
Vol 9 (3) ◽  
pp. 1324-1326 ◽  
Author(s):  
D R Katzenberg ◽  
S A Tilley ◽  
B K Birshtein

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.


Sign in / Sign up

Export Citation Format

Share Document