Isolation of two pure polysaccharides from the hemicellulose of slash pine (Pinus elliottii)

Two pure, acidic polysaccharides have been isolated from the hemicellulose of slash pine in yields of 1–2% and 4–5%. Their properties are compared, and the structure of one of them has been investigated by methylation analysis. The results indicate that the glycan is a β-D-(1→4)-linked xylan chain with many branch points. 4-O-Methyl-D-glucopyranosyluronic acid, L-arabinofuranose, and D-xylopyranose residues occur as non-reducing end groups. The uronic acid occurs as single-unit attachments to the main chain. Some of the D-xylose residues in the polysaccharide are doubly branched. The total hemicellulose components of the wood probably represent a complex mixture of chemical types, from which the two pure fractions described above may be separated fortuitously by careful, fractional precipitation.     

Application of Urine Analysis to Diagnosis and Treatment of Heroin Addiction

Experience with urine analysis for morphine using thin-layer chromatography in 310 cases of real or possible heroin abuse showed that it was valuable not only in detecting improper drug use but also in monitoring treatment. The results of this test can be available routinely in 24, and exceptionally in five hours. A negative result implies that the subject has taken less than 10 mg. of heroin in the past 24 hours.     

Histochemical detection of l-gulonolactone: phenazine methosulfate oxidoreductase activity in several mammals with special reference to synthesis of vitamin C in primates

Summary An improved detection of activity of l-gulonolactone oxidase, which is responsible for the final oxidative step in the synthetic process of l-ascorbate from glucose in animals, was achieved using phenazine methosulfate and cyanide. Cold acetone fixation eliminated non-specific deposition of formazan on lipid droplets. The specificity of the method was tested and proven by a biological control, histochemical controls, inhibitors and activators. By application of the method, strong reactivity was found in the cytoplasm of centrilobular parenchymal cells of livers of the opossum, rat, ground squirrel and flying squirrel. Staining of dog liver was moderate and centrilobular. Prosimians were strongly positive: The centrilobular localization was found in the tree shrew and galago; slow lorises and some pottos showed strong reactivity in centrilobular cells and some peripheral cells as well. These prosimians seem to be able to synthesize l-ascorbate as many lower mammals are. On the contrary, true simians (i.e. the squirrel monkey, spider monkey, rhesus monkey and chimpanzee) were negative as guinea pigs were, suggesting their probable inability for l-ascorbate synthesis.Visiting scientist from the Department of Anatomy, Tokyo Medical and Dental University, Tokyo, Japan. T. R. Shanthaveerappa in previous publications, also fellow, Department of Anesthesiology, Emory University.     

Histochemical studies on urate oxidase in several mammals with special reference to uricolytic ability of primates

Summary Strong reactivity for urate oxidase was found in the liver parenchymal cells of the prosimians (i.e. the tree shrew, slow loris, potto and galago) as well as those of lower mammals. The liver parenchymal cells of the platyrrhine monkeys (i.e. the marmoset, owl monkey, squirrel monkey, capuchin monkey and spider monkey) were moderately positive. There was no preferential distribution of granular reaction products in zones of liver lobules of these species. The prosimians and platyrrhine monkeys seem to be uricolytic as lower mammals are. On the other hand, the old world monkeys (i.e. Java monkey and rhesus monkey) and the apes (i.e. the orang-utan and chimpanzee) were histochemically negative.     

Studies on the distribution of phosphorylase in eyes of the rabbit and the squirrel monkey

Summary Detailed studies on phosphorylase localization in various components of the eyeball of rabbit and squirrel monkey have been made. Corneal epithelium, endothelium, and stromal cells, extrinsic and intrinsic muscles of the eyeball, ciliary process, endothelial cells of the anterior chamber angle, vitreal cells, lens epithelium, inner segment of cones; plexiform layer, ganglion cell layer, internal and external limiting membrane and Muller cells show high phosphorylase activity. Surprisingly, we observed phosphorylase activity inside the nucleus in the posterior 2 to 3 layers of corneal epithelium. The significance of phosphorylase localization in relation to glycogen distribution in various components of the eyeball and their energy requirements is stressed.