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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Characterization of a cobalamin-binding plasma protein from a patient with hepatoma. / Nexö, E; Olesen, H; Christensen, J M; Thomsen, J; Kristiansen, K.

In: Scandinavian Journal of Clinical & Laboratory Investigation, Vol. 35, No. 7, 1975, p. 683-90.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Nexö, E, Olesen, H, Christensen, JM, Thomsen, J & Kristiansen, K 1975, 'Characterization of a cobalamin-binding plasma protein from a patient with hepatoma', Scandinavian Journal of Clinical & Laboratory Investigation, vol. 35, no. 7, pp. 683-90. <http://www.ncbi.nlm.nih.gov/pubmed/174188>

APA

Nexö, E., Olesen, H., Christensen, J. M., Thomsen, J., & Kristiansen, K. (1975). Characterization of a cobalamin-binding plasma protein from a patient with hepatoma. Scandinavian Journal of Clinical & Laboratory Investigation, 35(7), 683-90. http://www.ncbi.nlm.nih.gov/pubmed/174188

Vancouver

Nexö E, Olesen H, Christensen JM, Thomsen J, Kristiansen K. Characterization of a cobalamin-binding plasma protein from a patient with hepatoma. Scandinavian Journal of Clinical & Laboratory Investigation. 1975;35(7):683-90.

Author

Nexö, E ; Olesen, H ; Christensen, J M ; Thomsen, J ; Kristiansen, K. / Characterization of a cobalamin-binding plasma protein from a patient with hepatoma. In: Scandinavian Journal of Clinical & Laboratory Investigation. 1975 ; Vol. 35, No. 7. pp. 683-90.

Bibtex

@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",

}

RIS

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

VL - 35

SP - 683

EP - 690

JO - Scandinavian Journal of Clinical & Laboratory Investigation

JF - Scandinavian Journal of Clinical & Laboratory Investigation

SN - 0036-5513

IS - 7

ER -

ID: 11368673