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

E Nexö; H Olesen; J M Christensen; J Thomsen; K Kristiansen

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

E Nexö, H Olesen, J M Christensen, J Thomsen, K Kristiansen

17 Citations (Scopus)

Abstract

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 language	English
Journal	Scandinavian Journal of Clinical & Laboratory Investigation
Volume	35
Issue number	7
Pages (from-to)	683-90
Number of pages	7
ISSN	0036-5513
Publication status	Published - 1975
Externally published	Yes

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@article{8372a75013d311de8478000ea68e967b,

title = "Characterization of a cobalamin-binding plasma protein from a patient with hepatoma",

abstract = "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.",

author = "E Nex{\"o} and H Olesen and Christensen, {J M} and J Thomsen and K Kristiansen",

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",

year = "1975",

language = "English",

volume = "35",

pages = "683--90",

journal = "Scandinavian Journal of Clinical & Laboratory Investigation",

issn = "0036-5513",

publisher = "Taylor & Francis",

number = "7",

}

TY - JOUR

T1 - Characterization of a cobalamin-binding plasma protein from a patient with hepatoma

AU - Nexö, E

AU - Olesen, H

AU - Christensen, J M

AU - Thomsen, J

AU - Kristiansen, K

N1 - 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

PY - 1975

Y1 - 1975

N2 - 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.

AB - 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.

M3 - Journal article

C2 - 174188

SN - 0036-5513

VL - 35

SP - 683

EP - 690

JO - Scandinavian Journal of Clinical & Laboratory Investigation

JF - Scandinavian Journal of Clinical & Laboratory Investigation

IS - 7

ER -

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

Abstract

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