Abstract
The NADP-dependent isocitrate dehydrogenase from pig liver soluble fraction was purified over 500-fold with an overall yield of 25%. The purified enzyme, which is homogeneous by all the usual criteria, has a molecular weight of about 75000 and is composed of two identical subunits. This has been demonstrated by ultracentrifugation, fluorescence titration and peptide `fingerprinting'. The maximal turnover number, extinction coefficients at 280nm and 260nm and amino acid analysis are described.
Dates
Type | When |
---|---|
Created | 10 years ago (Aug. 10, 2015, 3:28 p.m.) |
Deposited | 3 years, 9 months ago (Nov. 26, 2021, 2:38 p.m.) |
Indexed | 1 year, 9 months ago (Nov. 23, 2023, 5:41 p.m.) |
Issued | 55 years, 2 months ago (June 1, 1970) |
Published | 55 years, 2 months ago (June 1, 1970) |
Published Print | 55 years, 2 months ago (June 1, 1970) |
@article{Illingworth_1970, title={Purification and properties of the nicotinamide–adenine dinucleotide phosphate-dependent isocitrate dehydrogenase from pig liver cytoplasm}, volume={118}, ISSN={0306-3283}, url={http://dx.doi.org/10.1042/bj1180253}, DOI={10.1042/bj1180253}, number={2}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Illingworth, J. A. and Tipton, K. F.}, year={1970}, month=jun, pages={253–258} }