O2-Polarographic Studies on Soluble and Mitochondrial Enzymes of Crithidia fasciculata; Glycerophosphate Enzymes*
CYRUS J. BACCHI
Haskins Laboratories, 305 East 43rd St., New York, N. Y. 10017, Dept. of Biological Sciences, Fordham Univ., Bronx, N. Y. 10458, and Dept. of Pharmacology, Hahnemann Medical College, Philadelphia, Pa. 19102
Search for more papers by this authorS. H. HUTNER
Haskins Laboratories, 305 East 43rd St., New York, N. Y. 10017, Dept. of Biological Sciences, Fordham Univ., Bronx, N. Y. 10458, and Dept. of Pharmacology, Hahnemann Medical College, Philadelphia, Pa. 19102
Search for more papers by this authorE. I. CIACCIO
Haskins Laboratories, 305 East 43rd St., New York, N. Y. 10017, Dept. of Biological Sciences, Fordham Univ., Bronx, N. Y. 10458, and Dept. of Pharmacology, Hahnemann Medical College, Philadelphia, Pa. 19102
Search for more papers by this authorS. M. MARCUS
Haskins Laboratories, 305 East 43rd St., New York, N. Y. 10017, Dept. of Biological Sciences, Fordham Univ., Bronx, N. Y. 10458, and Dept. of Pharmacology, Hahnemann Medical College, Philadelphia, Pa. 19102
Search for more papers by this authorCYRUS J. BACCHI
Haskins Laboratories, 305 East 43rd St., New York, N. Y. 10017, Dept. of Biological Sciences, Fordham Univ., Bronx, N. Y. 10458, and Dept. of Pharmacology, Hahnemann Medical College, Philadelphia, Pa. 19102
Search for more papers by this authorS. H. HUTNER
Haskins Laboratories, 305 East 43rd St., New York, N. Y. 10017, Dept. of Biological Sciences, Fordham Univ., Bronx, N. Y. 10458, and Dept. of Pharmacology, Hahnemann Medical College, Philadelphia, Pa. 19102
Search for more papers by this authorE. I. CIACCIO
Haskins Laboratories, 305 East 43rd St., New York, N. Y. 10017, Dept. of Biological Sciences, Fordham Univ., Bronx, N. Y. 10458, and Dept. of Pharmacology, Hahnemann Medical College, Philadelphia, Pa. 19102
Search for more papers by this authorS. M. MARCUS
Haskins Laboratories, 305 East 43rd St., New York, N. Y. 10017, Dept. of Biological Sciences, Fordham Univ., Bronx, N. Y. 10458, and Dept. of Pharmacology, Hahnemann Medical College, Philadelphia, Pa. 19102
Search for more papers by this authorAided by N. I. H. grant AI 07895-01 to S. H. Hutner. Most of this material is abstracted from a thesis submitted by C. J. Bacchi to the Graduate School, Dept. of Biological Sciences, Fordham Univ., in partial fulfillment of the requirements for the Ph.D. degree.
Abstract
SYNOPSIS. Mitochondrial and supernatant fractions were isolated from Crithidia fasciculata by grinding with neutral alumina and differential centrifugation. Supernatant fractions contained at least 2 NAD-linked enzymes: an α-glycerophosphate dehydrogenase and a malate dehydrogenase. The properties of these enzymes were investigated polarographically with phenazine ethosulfate acting as electron acceptor. Agaricic acid, cinnamic acid and p-NO2-cinnamic acid were specific inhibitors of the α-glycerophosphate dehydrogenase.
Succinate, malate, DL-α-glycerophosphate and NADH stimulated respiration of mitochondrial preparations; O2 uptake was greatest with succinate. KCN and antimycin A inhibited succinate respiration more than α-glycerophosphate respiration. Amytal did not affect succinate, α-glycerophosphate or NADH oxidation. The trypanocide suramin inhibited mitochondrial respiration at least 77% with each substrate. The relevance of these results to other members of the Trypanosomatidae is discussed.
Abbreviations in this paper:
-
- α-GP
-
- α-glycerophosphate
-
- DHAP
-
- dihydroxyacetone phosphate
-
- NAD
-
- nicotinamide adenine dinucleotide
-
- PES
-
- phenazine ethosulfate
-
- MDH
-
- malate dehydrogenase
-
- NADP
-
- nicotinamide adenine dinucleotide phosphate
-
- FMN
-
- flavin mononucleotide
-
- FAD
-
- flavin adenine dinucleotide; antimycin, antimycin A
-
- ATP
-
- adenosine triphosphate
-
- ADP
-
- adenosine diphosphate
-
- EDTA
-
- ethylenediaminetetraacetic acid.
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