STRUCTURAL STUDIES OF MOUSE IMMUNOGLOBULIN GENES

1980 ◽  
pp. 27-33
Author(s):  
M. Steinmetz
Keyword(s):  
Immunoglobulin Genes ◽  
Structural Studies ◽  
Mouse Immunoglobulin

Optimization of primers for cloning libraries of mouse immunoglobulin genes using the polymerase chain reaction

1993 ◽  
Vol 23 (1) ◽  
pp. 206-211 ◽  
Author(s):  
Catherine A. Kettleborough ◽  
José Saldanha ◽  
Keith H. Ansell ◽  
Mary M. Bendig
Keyword(s):  
Polymerase Chain Reaction ◽  
Immunoglobulin Genes ◽  
Chain Reaction ◽  
Mouse Immunoglobulin ◽  
Polymerase Chain

scholarly journals Precise and in situ genetic humanization of 6 Mb of mouse immunoglobulin genes

2014 ◽  
Vol 111 (14) ◽  
pp. 5147-5152 ◽  
Author(s):  
L. E. Macdonald ◽  
M. Karow ◽  
S. Stevens ◽  
W. Auerbach ◽  
W. T. Poueymirou ◽  
...  
Keyword(s):  
Immunoglobulin Genes ◽  
Mouse Immunoglobulin

scholarly journals Chromosomal locations of mouse immunoglobulin genes.

1978 ◽  
Vol 75 (6) ◽  
pp. 2883-2887 ◽  
Author(s):  
O. Valbuena ◽  
K. B. Marcu ◽  
C. M. Croce ◽  
K. Huebner ◽  
M. Weigert ◽  
...  
Keyword(s):  
Immunoglobulin Genes ◽  
Mouse Immunoglobulin

Mouse Immunoglobulin Genes

1981 ◽  
pp. 157-188 ◽  
Author(s):  
P. Early ◽  
L. Hood
Keyword(s):  
Immunoglobulin Genes ◽  
Mouse Immunoglobulin

scholarly journals Structural Studies of a Heavy Chain from a Mouse Immunoglobulin M with Antibody Activity

1973 ◽  
Vol 248 (20) ◽  
pp. 7112-7117
Author(s):  
Elizabeth A. Robinson ◽  
Ettore Appella ◽  
K. Robert McIntire
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin M ◽  
Antibody Activity ◽  
Structural Studies ◽  
Mouse Immunoglobulin

scholarly journals Rapid removal of acetimidoyl groups from proteins and peptides. Applications to primary structure determination

1981 ◽  
Vol 199 (2) ◽  
pp. 335-340 ◽  
Author(s):  
G C Dubois ◽  
E A Robinson ◽  
J K Inman ◽  
R N Perham ◽  
E Appella
Keyword(s):  
Amino Acid ◽  
Primary Structure ◽  
Half Life ◽  
Structural Studies ◽  
Amino Groups ◽  
Mouse Immunoglobulin ◽  
Lysine Residues ◽  
Rapid Removal ◽  
Proteins And Peptides

Methylamine buffers can be used for the rapid quantitative removal of acetimidoyl groups from proteins and peptides modified by treatment with ethyl or methyl acetimidate. The half-life for displacement of acetimidoyl groups from fully amidinated proteins incubated in 3.44 M-methylamine/HCl buffer at pH 11.5 and 25 degrees C was approx. 26 min; this half life is 29 times less than that observed in ammonia/HCl buffer under the same conditions of pH and amine concentration. Incubation of acetimidated proteins with methylamine for 4 h resulted in greater than 95% removal of acetimidoyl groups. No deleterious effects on primary structure were detected by amino acid analysis or by automated Edman degradation. Reversible amidination of lysine residues, in conjunction with tryptic digestion, has been successfully applied to the determination of the amino acid sequence of an acetimidated mouse immunoglobulin heavy chain peptide. The regeneration of amino groups in amidinated proteins and peptides by methylaminolysis makes amidination a valuable alternative to citraconoylation and maleoylation in structural studies.

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