The presence of glycollate oxidase and dehydrogenase in Dunaliella primolecta

N.A. Nimer; A.-K.J. Sallal; R.H. Al-Hasan; M.J. Merrett

doi:10.1007/bf00195890

The presence of glycollate oxidase and dehydrogenase in Dunaliella primolecta

Planta ◽

10.1007/bf00195890 ◽

1990 ◽

Vol 181 (3) ◽

Cited By ~ 4

Author(s):

N.A. Nimer ◽

A.-K.J. Sallal ◽

R.H. Al-Hasan ◽

M.J. Merrett

Keyword(s):

Glycollate Oxidase

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Glycollate oxidase in Chlorella pyrenoidosa

Biochimica et Biophysica Acta (BBA) - Enzymology ◽

10.1016/0005-2744(68)90140-x ◽

1968 ◽

Vol 159 (3) ◽

pp. 543-544 ◽

Cited By ~ 13

Author(s):

M.J. Lord ◽

M.J. Merrett

Keyword(s):

Chlorella Pyrenoidosa ◽

Glycollate Oxidase

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The Identification of the Enzymes That Catalyse the Oxidation of Glyoxylate to Oxalate in the 100 000 g Supernatant Fraction of Human Hyperoxaluric and Control Liver and Heart Tissue

Clinical Science ◽

10.1042/cs0440227 ◽

1973 ◽

Vol 44 (3) ◽

pp. 227-241 ◽

Cited By ~ 23

Author(s):

Dorothy A. Gibbs ◽

R. W. E. Watts

Keyword(s):

Lactate Dehydrogenase ◽

Nicotinamide Adenine Dinucleotide ◽

Liver Tissue ◽

Primary Hyperoxaluria ◽

Heart Tissue ◽

Supernatant Fraction ◽

Glycollate Oxidase ◽

And Control ◽

Oxalate Synthesis ◽

Lactate Dehydrogenase Isoenzymes

1. The enzymic oxidation of glyoxylate to oxalate in the soluble (100 000 g supernatant) fraction of liver and heart tissue from a patient with primary hyperoxaluria and from a non-hyperoxaluric subject have been studied. 2. An oxidized nicotinamide—adenine dinucleotide (NAD+)-dependent and a non-NAD+-dependent oxidation of glyoxylate to oxalate were observed in the liver tissue from both sources. 3. Evidence is presented that lactate dehydrogenase has a major role in catalysing the reaction in both of the tissues studied. The non-NAD+-dependent oxidations which are catalysed by xanthine oxidase and glycollate oxidase in the liver are relatively unimportant, and they were not detected in the heart. 4. An enzyme that catalyses the oxidation of glycollate was also demonstrated in liver tissue. This had a different electrophoretic mobility from the lactate dehydrogenase isoenzymes. 5. These findings are discussed with particular reference to human primary hyperoxaluria in which excessive oxalate synthesis occurs.

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