Abstract
A specific protein exhibiting immunological cross-reactivity with chicken riboflavin carrier protein has been purified to homogeneity from human amniotic fluid by use of ion-exchange and affinity chromatography. The protein is similar to its avian counterpart in terms of molecular size, distribution of 125I-labelled tryptic peptides during finger printing, and preferential binding to riboflavin. Immunologically, they are homologous since most of the monoclonal antibodies raised against the avian protein cross-react with the purified human vitamin carrier.
Original language | English (US) |
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Pages (from-to) | 385-395 |
Number of pages | 11 |
Journal | Biochemistry International |
Volume | 27 |
Issue number | 3 |
State | Published - Jan 1 1992 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry