Characterization of antibodies to chicken riboflavin carrier protein: Antigenicity of the tryptic fragments.
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Date
1990-12
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Abstract
The antigenecity of tryptic fragments of reduced and carboxymethylated
chicken riboflavin carrier protein were studied. The tryptic sites of the native riboflavin
carrier protein bound to riboflavin were inaccessible. The molecular weight and the elution
profile on high performance liquid chromatography (TSK 545 DEAE) were unaltered at an
enzyme to substrate ratio of 1:31. However, carboxymethylated riboflavin carrier protein
could be cleaved into 3 or 4 fragments at an enzyme to substrate ratio of 1:250 or 1:125.
Chromatographic separation of the tryptic fragments on high pressure liquid
chromatography (TSK 545 DEAE) revealed the presence of two fragments with different
elution profiles but similar molecular weight 26 ±2 kDa. Only one fragment (associated
with peak 2) had the ability to displace chicken riboflavin carrier protein in an homologous
chicken riboflavin carrier protein radioimmunoassay. Thus, carboxymethylated ribotlavin
carrier protein which does not compete with chicken riboflavin carrier protein in the
radioimmunoassay, on mild trypsinization generates a fragment which interacts with
chicken riboflavin carrier protein in radioimmunoassay.
Description
Keywords
Riboflavin carrier protein, tryptic fragments, antigenicity
Citation
Natraj Usha, Iyer K S N, Raghavan Vijaya, Mahale Smita, Pereira Jacintha. Characterization of antibodies to chicken riboflavin carrier protein: Antigenicity of the tryptic fragments. Journal of Biosciences. 1990 Dec; 15(4): 341-350.