Identification of N5-methyl-N5-formyl-2,5,6-triamino-4-hydroxypyrimidine as a major adduct in rat liver DNA after treatment with the carcinogens, N,N-dimethylnitrosamine or 1,2-dimethylhydrazine

Human Tamm-Horsfall urinary glycoprotein from an individual of the blood group Sd(a+) phenotype was tritium-labelled by treatment with galactose oxidase and sodium boro[3H]hydride and was then digested with endo-beta-galactosidase. A series of dialysable, labelled fragments was released from which a pentasaccharide was isolated that strongly inhibited the agglutination of Sd(a+) red cells by human anti-Sda serum and hence contained the Sda determinant structure. Reduction, methylation analysis and sequential exo-glycosidase digestion established the structure of the pentasaccharide as: GalNAc beta(1 leads to 4)[NeuAc(2 leads to 3)]Gal beta(1 leads to 4)GlcNAc beta(1 leads to 3)Gal     

Interaction of ethanol with opiate receptors

Addition of ethanol to rat brain homogenate containing opiate receptors inhibits at a concentration of 50 mM the stereospecific binding of 3H-naloxone at 37 degrees C but not at 0 degree C, with the ID50 being 462 mM under these conditions. The temperature-dependent inhibition of the ligand binding suggests that ethanol does not compete with naloxone for specific binding sites of opiate receptors and changes the structure of lipids in biological membranes. Scatchard's analysis has demonstrated that apart from a decrease in the number of highly affinity binding sites of 3H-naloxone, the total amount of the binding sites remains unchanged both in the presence and absence of ethanol and constitutes 453 and 549 fmol/mg protein. It is assumed that ethanol might interconvert highly and low-affinity binding sites. Analysis of the effect of ethanol on 3H-naloxone binding with opiate receptors contained by synaptic membranes obtained from animals with varying predisposition to voluntary alcoholization has shown that ethanol inhibits to a greater degree ligand binding with membranes obtained from rats predisposed to alcoholization. The possibility of the involvement of receptors in the biochemical mechanisms by which the initial alcoholic motivation is effected is under discussion.     

Surface Plasmodium sugar-binding components evidenced by fluorescent neoglycoproteins

A sugar-binding component was shown to be present at the surface of endoerythrocytic Plasmodium berghei and P. chabaudi stages and merozoites by means of a panel of neoglycoproteins using fluorescence microscopy and flow cytofluorometry. The protein nature of this material was ascertained by the loss of sugar-binding capacity upon trypsin treatment. This lectin-like protein primarily bound neoglycoprotein-borne N-acetylglucosamine and secondarily bound neoglycoprotein-borne alpha-D-glucose, beta-D-galactose and alpha-L-fucose. These results suggest the presence of at least one type of lectin-like protein with an extended binding site accomodating several sugar units, and define its localization on the parasite surface.     

Effect of adrenaline on kidney lysosome function in rats during prolonged soft tissue crushing

The total and unsedimentable activity of acid DNase, RNase, phosphatase and arylsulfatases A and B was examined in the rat kidneys during long-term compression of soft tissues in the presence of high excitability of the sympathoadrenal system. Injection of adrenalin to rats with trauma reduced the total activity of DNase, acid phosphatase and arylsulfatases A and B, particularly at the late periods of soft tissue compression, whereas the total activity of acid RNase slightly increased as compared with control. Compression of soft tissues after adrenalin preinjection was accompanied by a substantial rise of unsedimentable activity of the lysosomal enzymes under study in the kidneys. The activity of the enzymes in cytosol progressively ascended as the time of soft tissue injury increased.     

A radioimmunoassay for epinephrine and norepinephrine in tissues and plasma

An I¹²⁵ radioimmunoassay (RIA) has been developed for the measurement of plasma and tissue epinephrine (E) and norepinephrine (NE). The assay utilizes an antibody which specifically binds metanephrine. E and NE are detected by conversion to metanephrine with the enzymes catechol-0-methyltransferase and phenylethanol-amine-N-methyltransferase. The assay is very specific and will allow the measurement of E and NE in less than 500 μl of normal human plasma. E and NE concentrations were determined by both the RIA and a radioenzymatic assay in canine, human and rat biologic samples. The correlation coefficients between the two assays were .962 for E and .956 for NE. The RIA is sensitive, specific, precise and significantly less costly and time consuming than present radioenzymatic methods.     

Identification of bacteria of dairy origin using miniaturized test-systems

One hundred and forty-four isolates of dairy origin were identified using a number of commercially available test kits. Agreement between these kits was acceptable for assignment of isolates to genera, but there was some variation between the kits for the identification of the isolates at specific level. The reasons for these variations are discussed. In terms of cost, ease of performance and accuracy, the identification systems manufactured by Roche Products Ltd (viz. the Oxi/Ferm tube and the Enterotube) are considered to be the best suited to the routine identification of dairy micro-organisms.     

Study in the anuran amphibian Xenopus laevis, some blood characteristics and nitrogen excretion based on changes in the water osmolarity]

The pH, the osmolality and the urea and ammonia concentrations in blood, as well as the net urea and ammonia excretions, were studied in the amphibian Xenopus laevis exposed for several weeks to increased osmotic pressure (OP) of the ambient water, as a result of the addition of either NaCl or mannitol to the water. The pH and the ammonia concentration of the blood were independent of the variations of the ambient osmolarity. On the contrary, the blood osmolality and its urea concentration increased markedly when the ambient OP was augmented. The increase of ambient OP by NaCl addition to the medium augmented the urea net excretion and slightly decreased the ammonia excretion. When the increase of ambient OP resulted from the addition of mannitol in the water, excretions of urea and ammonia became negligible.