The excretion of urinary N-acetyl-beta-glucosaminidase and beta-glucuronidase as a sign of impending rejection of kidney transplants.

An evaluation was made of the assay of two urinary lysosomal enzymes, N-acetyl-beta-glucosaminidase and beta-glucuronidase, in the diagnosis of impending rejection of renal transplant. The output of enzymes was measured in 34 cadaver transplant recipients, 17 of whom underwent rejection episodes. The enzyme output during the 4 days preceding the definitive diagnosis was compared with the output during a non-rejection period.

Effect of a low-protein diet on acetaldehyde metabolism in rats.

The effect of dietary changes on liver alcohol and aldehyde dehydrogenase activities as related to effects on ethanol and acetaldehyde metabolism was investigated. Feeding rats for 8 weeks on diets rich in carbohydrate or fat, but with normal protein content, induced minor changes relative to giving a balanced diet. A low-protein, high-carbohydrate diet (5 per cent and 80 per cent of calory content, respectively) caused a significant reduction of both alcohol and aldehyde dehydrogenase activities in the liver.

Role of cytosolic rat liver aldehyde dehydrogenase in the oxidation of acetaldehyde during ethanol metabolism in vivo.

The activity of a high-Km aldehyde dehydrogenase in the liver cytosol was increased by phenobarbital induction. No corresponding increase in the oxidation rate of acetaldehyde in vivo was found, and it is concluded that cytosolic aldehyde dehydrogenase plays only a minor role in the oxidation of acetaldehyde during ethanol metabolism.

Partial purification and properties of a phenobarbital-induced aldehyde dehydrogenase of rat liver.

Properties of the phenobarbital induced cytoplasmic aldehyde dehydrogenase (EC 1.2.1.

Different forms of rat liver aldehyde dehydrogenase and their subcellular distribution.

1. The properties and distribution of the NAD-linked unspecific aldehyde dehydrogenase activity (aldehyde: NAD+ oxidoreductase EC 1.2.