Leucine aminopeptidase in extracts of swine muscle

1. Leucine aminopeptidase (EC 3.4.1.1) has been demonstrated in swine muscle at a level of activity one-fifth that of the swine kidney. 2. The enzyme has been purified 110-fold by precipitation with ammonium sulphate, heat treatment and chromatography on Sephadex G-100. 3. The enzyme is heat-stable, but is rapidly inactivated below pH7. It requires Mg(2+) or Mn(2+) for activity. The Michaelis constant for leucine amide with Mg(2+)-activated enzyme is 5.0x10(-3)m. 4. Muscle leucine aminopeptidase is very similar to the kidney enzyme.     

The Medical and Human Performance Problems of Living Under the Sea

Recent undersea experiments in the United States and France showed that divers can live and work effectively for many days from dwellings placed on the continental shelf to depths down to 432 feet. If prolonged exposure to the hostile underwater environment is to be tolerated successfully, existing physical, biological and equipment hazards must be recognized, prepared for and, when possible, circumvented.     

CLINICAL OBSERVATIONS ON IPRONIAZID IN IDIOTS WITH EPILEPSY

In contradistinction to the observation made before that iproniazid has a potentiating effect on certain amines in guinea pigs, human studies have shown that this effect has very little clinical importance, when both the amines and the amine oxidase inhibitor are given in the usual therapeutic doses. However, neither in man nor in the guinea pig pretreatment with iproniazid showed a potentiating effect on amines which are not substrates of monoamine oxidase (ephedrine and amphetamine). Patients with epilepsy and allergic disease may receive iproniazid.