Characterization of a cobalamin-binding plasma protein from a patient with hepatoma

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A cobalamin-binding protein has been purified by affinity chromatography from plasma of a patient with hepatoma and a 10,000-fold increase in the concentration of the plasma cobalamin-binding capacity. The protein behaved as normal transcobalamin I in gel filtration, agar gel electrophoresis, immunoelectrophoresis, precipitation by ammonium sulphate, and cobalamin-binding studies. The protein contained 38 per cent carbohydrate, and the relative molecular mass based on amino acid and carbohydrate analyses was 69,000. The molar absorption coefficient of cyanocobalamin bound to the protein was determined to be 36,000 at 362 nm. On amino acid sequencing, one amino terminal was found, and the first 13 residues were determined as Glu-Ile-Ser/Cys-Glu-Val-Ser/Cys-Glu-Glu-Asx-Tyr-Ile-Arg-Leu/Ile.
Original languageEnglish
JournalScandinavian Journal of Clinical & Laboratory Investigation
Issue number7
Pages (from-to)683-90
Number of pages7
Publication statusPublished - 1975
Externally publishedYes

Bibliographical note

Keywords: Amino Acid Sequence; Amino Acids; Carbohydrates; Carcinoma, Hepatocellular; Carrier Proteins; Chromatography, Affinity; Electrophoresis, Agar Gel; Humans; Immunoelectrophoresis; Liver Neoplasms; Molecular Weight; Protein Binding; Transcobalamins; Vitamin B 12

ID: 11368673