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M Agosin

Publications and source records attributed to M Agosin.

46 records · Page 3Linked to original sources

Echinococcus antigens.

Much of the work on immunology of hydatidosis has so far been devoted to the development of suitable methods for serological diagnosis. The precise nature of hydatid antigens and their chemical characterization has still not been worked out, largely because of the complex life-history of the parasite and the difficulties of in vitro cultivation. The most widely used antigen for routine serological testing in hydatidosis caused by Echinococcus granulosus is fluid taken from the cyst. This fluid is, however, a complex mixture of substances and contains several protein and carbohydrate fractions as well as end-products of carbohydrate and protein metabolism. The cyst fluid from different sources is variable in its antigenic properties, and the fluid from sterile cysts is especially lacking in antigenic activity. Antigens from tissue extracts of hydatid cysts appear to have greater specificity. Cyst extracts of E. multilocularis, the cysts of which contain relatively little fluid, have also been used but are poor antigens, and contain measurable amounts of host protein. Antigens prepared from other cestodes and metabolic antigens are also reviewed.Biochemical analysis of Echinococcus antigens covering polysaccharides, proteins, lipids, and blood-group substances is considered, together with the characterization of antigens by electrophoresis, column chromatography and gel-diffusion methods. The problems associated with the standardization of antigens are discussed. Recent data on the character and reactivity of antigens employed in Echinococcus studies are summarized.

Antigens↗

Conversion of N,N-dimethylaniline to N,N-dimethylaniline-N-oxide by a cytosolic flavin-containing enzyme from Trypanosoma cruzi.

A cytosolic NADPH-dependent FAD-containing enzyme purified from Trypanosoma cruzi epimastigotes [Kuwahara, White, and Agosin: Biochem. Biophys. Res. Commun. 124, 121 (1984); Arch. Biochem. Biophys. 239, 18 (1985)] catalyzes the conversion of N,N-dimethylaniline to its corresponding N-oxide. The identity of the product has been established by high performance liquid chromatography and paper chromatography elution patterns and by electron impact spectrometry. The oxidation of N,N-dimethylaniline was determined by following the oxidation of NADPH spectrophotometrically, and a double reciprocal plot of reaction velocity vs. substrate concentration was prepared. At an optimum pH of 8.0, the plot resulted in Km and Vmax values of 56 microM and 114 nmol X min-1 X mg of protein-1, respectively. The oxidative activity of the enzyme suggests that it may be involved in detoxication processes which may contribute to the resistance of T. cruzi to known antiprotozoal drugs.

Aniline Compounds↗

Methoprene and hydroprene are metabolized by ester cleavage in isolated hepatocytes.

Methoprene (isopropyl [2E,4E]-11-methoxy-3,7,11-trimethyldodeca-2,4-dienoate) and hydroprene (ethyl[2E,4E]-3,7,11-trimethyldodeca-2,4-dienoate) are actively metabolized, mainly to their corresponding acids by isolated rat hepatocytes and rat liver subcellular fractions. Small amounts of conjugates corresponding to glucuronides are also found. The esterase activity is of microsomal origin and is almost completely inhibited by tri-o-tolyl phosphate in isolated hepatocytes and microsomal fractions supplemented with NADPH. No evidence for the participation of the NADPH-dependent cytochrome P-450 system in the metabolism of either compound was observed.

Animals↗