May 15, 1976

The effects of proteolytic digestion by trypsin on the structure and catalytic properties of reduced nicotinamide-adenine dinucleotide dehydrogenase from bovine heart mitochondria

The Biochemical Journal
C I Ragan

Abstract

1. At 21 degrees C incubation of NADH-ubiquinone-1 reductase (Complex 1) with trypsin caused selective inhibition of nicotinamide nucleotide transhydrogenase activity. The reduction of K3Fe(CN)6 by NADH or NADPH was unaffected, but a slow decrease in the rate of reduction of ubiquinone-1 by NADH was observed. 2. The pH-dependence of nicotinamide nucleotide transhydrogenase activity differed in Complex I and trypsin-treated Complex I. The trypsin-labile activity had a pH optimum of approx. 6.5, whereas the trypsin-resistant activity had a pH optimum of approx. 5.5 or less. 3. The trypsinlabile transhydrogenase activity was specifically inhibited by butanedione or phenylglyoxal and was identified with the enzyme catalysing energy-linked transhydrogenase activity in submitochondrial particles. 4. Polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate revealed that trypsin caused degradation of a polypeptide of mol.wt 20500 in parallel with the loss of transhydrogenase activity. 5. At 30 degrees C and higher trypsin concentrations, the rate of reduction of K3Fe(CN)6 by NADH or NADPH slowly decreased. Increased lability of NADH-K3Fe(CN)6 reductase activity to trypsin was observed when the endogenous phospholip...Continue Reading

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Mentioned in this Paper

Ubiquinone (Lab Procedure)
NAD(P)+ Transhydrogenase Activity
Bos taurus
Mitochondria, Heart
Myocardium
Phospholipase A Activity
NADH
Proteolytic Enzyme
Trypsin
Nicotinamide Nucleotide Transhydrogenase Activity

About this Paper

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