Immobilized purified folate-binding protein: binding characteristics and use for quantifying folate in erythrocytes
Abstract
Purified folate-binding protein from cow's milk was immobilized on monodisperse polymer particles (Dynospheres) activated by rho-toluenesulfonyl chloride. Leakage from the spheres was less than 0.1%, and the binding properties were similar to those of the soluble protein with regard to dissociation, pH optimum for binding pteroylglutamic acid, and specificity for binding various folate derivatives. We used the immobilized folate-binding protein as binding protein in an isotope-dilution assay for quantifying folate in erythrocytes. The detection limit was 50 nmol/L and the CV over a six-month period was 2.3% (means = 1.25 mumol/L, n = 15). The reference interval, for folate measured in erythrocytes of 43 blood donors, was 0.4-1.5 mumol/L.
- Authors:
- Publication Date:
- Research Org.:
- Central Hospital, Hillerod, Denmark
- OSTI Identifier:
- 6025342
- Resource Type:
- Journal Article
- Journal Name:
- Clin. Chem. (Winston-Salem, N.C.); (United States)
- Additional Journal Information:
- Journal Volume: 33:8
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; FOLIC ACID; BIOCHEMICAL REACTION KINETICS; PROTEINS; CHEMICAL PROPERTIES; CATTLE; ERYTHROCYTES; ISOTOPE DILUTION; MILK; POLYMERS; SPECIFICITY; AMINO ACIDS; ANIMALS; AROMATICS; AZAARENES; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BODY FLUIDS; CARBOXYLIC ACIDS; DOMESTIC ANIMALS; DRUGS; FOOD; HEMATINICS; HEMATOLOGIC AGENTS; HETEROCYCLIC COMPOUNDS; HYDROXY COMPOUNDS; ISOTOPE APPLICATIONS; KINETICS; MAMMALS; MATERIALS; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; PTERIDINES; REACTION KINETICS; RUMINANTS; TRACER TECHNIQUES; VERTEBRATES; VITAMIN B GROUP; VITAMINS; 550201* - Biochemistry- Tracer Techniques
Citation Formats
Hansen, S I, Holm, J, and Nexo, E. Immobilized purified folate-binding protein: binding characteristics and use for quantifying folate in erythrocytes. United States: N. p., 1987.
Web.
Hansen, S I, Holm, J, & Nexo, E. Immobilized purified folate-binding protein: binding characteristics and use for quantifying folate in erythrocytes. United States.
Hansen, S I, Holm, J, and Nexo, E. 1987.
"Immobilized purified folate-binding protein: binding characteristics and use for quantifying folate in erythrocytes". United States.
@article{osti_6025342,
title = {Immobilized purified folate-binding protein: binding characteristics and use for quantifying folate in erythrocytes},
author = {Hansen, S I and Holm, J and Nexo, E},
abstractNote = {Purified folate-binding protein from cow's milk was immobilized on monodisperse polymer particles (Dynospheres) activated by rho-toluenesulfonyl chloride. Leakage from the spheres was less than 0.1%, and the binding properties were similar to those of the soluble protein with regard to dissociation, pH optimum for binding pteroylglutamic acid, and specificity for binding various folate derivatives. We used the immobilized folate-binding protein as binding protein in an isotope-dilution assay for quantifying folate in erythrocytes. The detection limit was 50 nmol/L and the CV over a six-month period was 2.3% (means = 1.25 mumol/L, n = 15). The reference interval, for folate measured in erythrocytes of 43 blood donors, was 0.4-1.5 mumol/L.},
doi = {},
url = {https://www.osti.gov/biblio/6025342},
journal = {Clin. Chem. (Winston-Salem, N.C.); (United States)},
number = ,
volume = 33:8,
place = {United States},
year = {Sat Aug 01 00:00:00 EDT 1987},
month = {Sat Aug 01 00:00:00 EDT 1987}
}