Isolation and characterization of riboflavin carrier protein from human amniotic fluid

Puttur D Prasad, P. Malhotra, A. A. Karande, P. R. Adiga

Research output: Contribution to journalArticle

9 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)385-395
Number of pages11
JournalBiochemistry International
Volume27
Issue number3
StatePublished - Jan 1 1992
Externally publishedYes

Fingerprint

Amniotic Fluid
Avian Proteins
Affinity chromatography
Printing
Fluids
Riboflavin
Ion Exchange Chromatography
Affinity Chromatography
Vitamins
Fingers
Chickens
Ion exchange
Proteins
Monoclonal Antibodies
Peptides
riboflavin-binding protein

ASJC Scopus subject areas

  • Biochemistry

Cite this

Isolation and characterization of riboflavin carrier protein from human amniotic fluid. / Prasad, Puttur D; Malhotra, P.; Karande, A. A.; Adiga, P. R.

In: Biochemistry International, Vol. 27, No. 3, 01.01.1992, p. 385-395.

Research output: Contribution to journalArticle

Prasad, Puttur D ; Malhotra, P. ; Karande, A. A. ; Adiga, P. R. / Isolation and characterization of riboflavin carrier protein from human amniotic fluid. In: Biochemistry International. 1992 ; Vol. 27, No. 3. pp. 385-395.
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