๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Enzymes in cancer. II. The isocitric dehydrogenase of the cerebrospinal fluid in various cancerous and noncancerous conditions

โœ Scribed by Marc van Rymenant; Jacques Robert


Publisher
John Wiley and Sons
Year
1960
Tongue
English
Weight
352 KB
Volume
13
Category
Article
ISSN
0008-543X

No coin nor oath required. For personal study only.

โœฆ Synopsis


SOCITRIC dehydrogenase is the enzyme that I catalyzes the transformation of isocitrate into a-ketoglutarate. Wolfson and Williams-Ashman and their collaborators29 3 have demonstrated the presence of this enzyme in human serum and shown that its activity is elevated in cases of hepatitis or metastatic liver cancer but not in cases of obstructive jaundice. By using the same technique of measurement, but at a different temperature, we have demonstrated the presence of this enzyme in the cerebrospinal fluid, and we have studied its variation in pathological conditions of the nervous system, especially in tumors.

MATERIAL AND METHODS

The following reagents were used: (1) sodium isocitrate in a concentration of 32.x 1WM; (2) triphosphopyridine nucleotide (TPN) in a concentration of 1 . 2 9 x l V M ; and

(3) manganese chloride in a concentration of 19.x 1 W M .

T h e buffer solution consisted of 0.2M triethanolamine and hydrochloric acid at pH 7.5.

T h e method of measurement was essentially the same as that used by Wolfson and Williams-Ashman and their co-worker& 3 with the following changes: the measurement was carried out on 2 ml. of spinal fluid in a volume of reaction mixture of 4.1 ml. at 37" C. Distilled water was used as a blank.

Standardization. As in the method of Wolfson and Williams-Ashman and their collabo-


๐Ÿ“œ SIMILAR VOLUMES


Effects of wild-type p53 expression on t
โœ Daniel Hochhauser; Nikola I. Valkov; Jana L. Gump; Irene Wei; Carolyn O'Hare; Jo ๐Ÿ“‚ Article ๐Ÿ“… 1999 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 455 KB ๐Ÿ‘ 1 views

The p53 null HL-60 cell line was transfected with plasmids coding for either the wild-type p53 or mutant p53 gene. The stable expression of wild-type p53 resulted in a significant increase in sensitivity to the topoisomerase II poisons etoposide and doxorubicin, but not to the topoisomerase II inhib