Purification and comparative properties of isoenzymes of nicotinamide-adenine dinucleotide phosphate-isocitrate dehydrogenase from rat heart and liver.

Content Provider	Semantic Scholar
Author	Islam, M. Bell, Joyce L. Baron, D. N.
Copyright Year	1972
Abstract	1. Rat liver and heart major isoenzymes of NADP-isocitrate dehydrogenase have each been purified about 100-fold by a combination of ammonium sulphate fractionation and chromatography on ion-exchange cellulose and their properties compared. 2. The properties were similar in respect of pH, inhibition by Hg(2+) and Michaelis constants for isocitrate and NADP. 3. Some of the properties of the isoenzymes were different. 4. The heart isoenzyme was activated about 210% by 0.8m-ammonium sulphate whereas the liver isoenzyme was unaffected. The heart isoenzyme showed greater sensitivity to inactivation by heat (30 degrees C for 30min), whereas the liver isoenzyme was more sensitive to inactivation by p-chloromercuribenzoate and by Cu(2+). 5. The Michaelis constants with 3-acetylpyridine-adenine dinucleotide phosphate showed a twofold difference between liver and heart isoenzyme. 6. The differential sensitivity to heat and its mainly non-cytoplasmic location may be an explanation of the failure of plasma isocitrate dehydrogenase activity to increase after a myocardial infarction.
File Format	PDF HTM / HTML
DOI	10.1042/bj1291003
PubMed reference number	4144230
Journal	Medline
Volume Number	129
Issue Number	5
Alternate Webpage(s)	http://www.biochemj.org/content/ppbiochemj/129/5/1003.full.pdf
Alternate Webpage(s)	https://doi.org/10.1042/bj1291003
Journal	The Biochemical journal
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article