Isoleucine and Valine Metabolism in Escherichia coli XVIII. Induction of Acetohydroxy Acid Isomeroreductase

The regulation by substrate induction of the acetohydroxy acid isomeroreductase was studied in Escherichia coli. Induction was inhibited by chloramphenicol and rifampin. The addition of rifampin resulted in a decay of the capacity to form isomeroreductase. This was attributed to the breakdown of the isomeroreductase messenger, which had a half-life of about 45 sec at 37 C. Induction of isomeroreductase was enhanced by including glucose in the medium. This effect was shown to be due in part to the lowering of the pH of the medium, which presumably made inducer entry more rapid.     

Observations on the Staining of Corynebacterium Diphtheriae

Albert's method, of staining diphtheria cultures consists of staining a fixed smear for one minute (some laboratories stain for five minutes) with a solution containing toluidine blue and malachite (or methyl) green, washing with water, and applying Albert's iodine for one minute. This procedure is discussed and criticized, and in addition the mechanism of the stain is elucidated. Also, the procedure which involves staining a fixed smear for one minute with Loeffler's alkaline methylene blue solution is discussed and criticized.

To overcome the objections to the above staining methods, a different method is proposed. This consists of staining a fixed smear with an acid solution of toluidine blue, washing with water, applying Albert's iodine for one minute, washing with water, and finally applying a safranin solution for 15-20 seconds. The theoretical basis for this method is presented.     

GABA UPTAKE IN RAT BRAIN SLICES: INHIBITION BY GABA ANALOGUES AND BY VARIOUS DRUGS

Abstract— 2-Hydroxy-, 2-chloro-, 2- and Cmethyl-GABA are linear competitive inhibitors of GABA uptake in rat brain slices. These analogues are thus potential substrates for the GABA transport system and possible'false transmitters'. 2-Hydroxy-GABA is the most potent inhibitor of GABA uptake yet described. No specific inhibitor of GABA uptake was revealed amongst the drugs tested.     

Localization of alkaline phosphatase and NADH diaphorase in the principal cells of the guinea pig epididymis

The activities of alkaline phosphatase and reduced nicotinamide adenine dinucleotide (NADH) diaphorase in the principal cells of the guinea pig epididymis were studied histochemically. Alkaline phosphatase activity was absent from the principal cells but was present in the basement membrane of the epididymal epithelium. NADH diaphorase activity was distributed throughout the cytoplasm of the principal cells in each epididymal segment. There was a gradual increase in NADH diaphorase activity from segments 1 through 7. Possible functions of alkaline phosphatase and NADH diaphorase in the epididymis are discussed.