The relationship between the CHE2 locus of serum cholinesterase (BChE) and adult human weight was studied in a sample of 225 CHE2 C5+ individuals and 225 CHE2 C5- controls matched for sex, height, age and race. With respect to the intensity of the C₅ band staining (scored 1–6), 113 individuals had faint C₅ bands (scores 1–3) and 112 intense C₅ bands (scores 4–6). The individuals with intense CHE2 C5+ phenotype showed a significantly lower mean adult weight (64.66 ± 0.73 kg) when compared to their controls (70.59 ± 0.97 kg) and a significant reduction in weight variance (59.81 and 105.18, respectively). Individuals with faint C₅ bands, although showing a negative correlation between weight and C₅ band intensity, did not differ from their controls in mean weight.

Growth of the fungus Pullularia pullulans on L-rhamnose induces the synthesis of L-rhamnofuranose dehydrogenase and other enzymes active in dissimilation of L-rhamnose (6-deoxy-L-mannose). The present findings indicate that at pH 7.0 a lactonase is active in the hydrolysis of L-rhamnono-γ-lactone. The resulting L-rhamnonate is then dehydrated into 2-keto-3-deoxy-L-rhamnonate by an L-rhamnonate dehydratase. It is also shown that, in the extracts, 2-keto-3-deoxy-L-rhamnonate aldolase participates in the catalysis of the cleavage of 2-keto-3-deoxy-L-rhamnonate to form pyruvate and L-lactaldehyde. The presence of D-glucose (0.2%) together with the inducer in the induction medium gives rise to approximately 50% repression of dehydrogenase synthesis, 80% repression of dehydratase synthesis, and 87% repression of aldolase synthesis. Induction of the enzymes of this nonphosphorylative pathway is completely inhibited in the presence of high levels of D-glucose (2%). It is suggested that these enzymes are active in the metabolism of L-rhamnose by the following pathway: L-rhamnose → L-rhamnono-γ-lactone → L-rhamnonate → 2-keto-3-deoxy-L-rhamnonate → pyruvate plus L-lactaldehyde, and that this is believed to be the route for L-rhamnose dissimilation in this microorganism.

The growth of Pullularia pullulans on L-rhamnose (6-deoxy-L-mannose) as the sole carbon source induces the synthesis of L-rhamnose dehydrogenase, a nicotinamide adenine dinucleotide-dependent enzyme that catalyzes the oxidation of the deoxy sugar to L-rhamnonolactone. The enzyme induction is inhibited by cycloheximide, suggesting de novo synthesis. The presence of D-glucose (0.2%) or D-galactose (0.2%) simultaneously with the inducer in the induction medium produced 50% repression of dehydrogenase synthesis, but no effect was detected with D-fructose and D-mannose at the same concentration. High levels of Dglucose (2%), under maximal catabolite repression conditions, produced a complete inhibition of enzyme synthesis.

The frequency of the CHE1*K allele was estimated as 2.04 ± 2.02% in a population sample from Southern Brazil. Previously reported estimates refer to the British population and are significantly higher than the present one. Our hypothesis is that the British frequencies may represent overestimates due to ascertainment conditions.

An improved method for the identification of butyrylcholinesterase phenotypes is proposed. It is based on modifications of a method that uses alpha-naphthyl acetate as substrate and DL-propranolol and Ro2-0683 as inhibitors. The proposed modifications make the method more rapid and increase the accuracy of the determinations of the phenotypes tested (BCHE U, BCHE UF, BCHE UA, BCHE AK, BCHE AF, and BCHE A). These modifications make the method even more adequate for population studies and clinical routine.