Characterization of antibodies to chicken riboflavin carrier protein: Antigenicity of the tryptic fragments

1990 ◽  
Vol 15 (4) ◽  
pp. 341-350 ◽  
Author(s):  
Usha Natraj ◽  
K. S. N. Iyer ◽  
Vijaya Raghavan ◽  
Smita Mahale ◽  
Jacintha Pereira
1988 ◽  
Vol 254 (1) ◽  
pp. 287-292 ◽  
Author(s):  
U Natraj ◽  
S George ◽  
M S Kadam

The properties of antibodies generated in rabbits against native riboflavin carrier protein (cRCP), riboflavin carrier protein that had been denatured/renatured by SDS treatment (SDS-RCP) or disulphide-bond-reduced then S-carboxymethylated (Carb-RCP) were studied. SDS-RCP could displace native RCP in radioimmunoassay (r.i.a.), whereas Carb-RCP could not. By using antibodies raised in five different rabbits against native cRCP, 125I-labelled Carb-RCP could bind between 0 and 30% of the native antibodies. Antibodies raised against native RCP appear to be largely directed towards specific conformational determinants of RCP. Carb-RCP displaced native RCP in an r.i.a. using antibodies raised against SDS-RCP. SDS denaturation presumably unmasks cryptic epitopes in native RCP. Carb-RCP was a weak immunogen and elicited, presumably, antibodies to sequential epitope/epitopes. When injected into pregnant mice the antibodies caused neutralization of RCP, leading to termination of pregnancy, indicating highly conserved sequential epitopes in chicken and rodent RCP. Antibodies raised against Carb-RCP or native RCP reacted with CNBr fragments of native RCP, further confirming the presence of sequence-specific antibodies elicited by Carb-RCP.


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