Published September 1983
| Version v1
Journal article
The influence of experimental conditions on the association constant for binding of vitamin B12 by human intrinsic factor coupled to Sepharose 4B
- 1. Rijksuniversiteit Utrecht (Netherlands). Analytisch Chemisch Lab.
Description
The association constant for binding of vitamin B12 (cyanocobalamin) by human intrinsic factor coupled to Sepharose 4B and the concentration of binding sites of the coupled intrinsic factor have been measured as a function of pH, temperature, ionic strength and the presence of various (ionic and non-ionic) components in the solution. (author)
Additional details
Publishing Information
- Journal Title
- Int. J. Appl. Radiat. Isot.
- Journal Volume
- 34
- Journal Issue
- 9
- Series
- Int. J. Appl. Radiat. Isot.
- Journal Page Range
- 1351-1356
- ISSN
- 0020-708X
INIS
- Country of Publication
- United Kingdom
- Country of Input or Organization
- United Kingdom
- INIS RN
- 15013410
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- BUFFERS; ENTHALPY; ENTROPY; INTRINSIC FACTOR; IONS; LIGANDS; MAN; PH VALUE; QUANTITY RATIO; SACCHARIDES; TEMPERATURE DEPENDENCE; VITAMIN B-12
- Descriptors DEC
- ANIMALS; CARBOHYDRATES; CHARGED PARTICLES; MAMMALS; MUCOPROTEINS; ORGANIC COMPOUNDS; PHYSICAL PROPERTIES; POLYSACCHARIDES; PRIMATES; PROTEINS; THERMODYNAMIC PROPERTIES; VERTEBRATES; VITAMIN B GROUP; VITAMINS