[Yeast peroxisomes (microbodies): structure, function and application (author's transl)].
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Biomedical subjects
Publications and source records attributed to A Tanaka.
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The antigenic differences among human cytomegalovirus (CMV), two laboratory strains (Davis, AD 169), isolates from pregnant women's cervical secretions, mother's milk, infants' throat swabs and urine were analyzed by means of the plaque reduction assay using human sera which were assumed to contain monotypic antibodies by primary infection and boosted antibodies by reinfection or reactivation of the latent virus. In the cross-neutralization tests, there were no remarkable differences among the CMV strains examined. Moreover, in the neutralization kinetics, normalized kappa values among the strains constantly exceeded 80. Therefore, it is suggested that the human CMV strains examined in the study were serologically identical or very closely related.
Muramyl dipeptide (MDP), a part of bacterial cell wall peptidoglycans, was active as adjuvant and stimulated the reticuloendothelial system (RES) of mice to increase its phagocytic function. A series of analogs of MDP was tested for their adjuvant activity and RES-stimulating activity. Sex differences were observed in the adjuvant activity and RES-stimulating capacity of some MDP analogs. A stereochemically highly specific structure required for MDP to exert adjuvant activity was also required for its RES-stimulating activity. Based on this close correlation among the structure, adjuvant activity, and RES-stimulating capacity of MDP, we infer that macrophages may play an important role in the expression of adjuvant activity of MDP.
In the capillary tube migration system a synthetic muramyl dipeptide (MDP; N-acetylmuramyl-L-alanyl-D-isoglutamine), a part of bacterial cell wall peptidoglycans, inhibited the migration of peritoneal exudate macrophages from normal guinea pigs or rats. The migration inhibition was also caused by some MDP-containing peptidoglycan fragments from cell walls of Lactobacillus plantarum and Staphylococcus epidermidis. The migration inhibition could not be explained on the basis of macrophage migration inhibitory factor. A stereochemically highly specific structure of MDP required for its adjuvant activity was also required for the macrophage migration inhibition. These findings suggest that MDP and MDP-containing cell wall fragments may activate macrophages and that this activation may be important in the exertion of their adjuvant activity.
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Anomeric forms of glucose produced from phenyl alpha-maltoside, maltose, or phenyl alpha-glucoside have been determined quantitatively by simultaneous measurements of optical rotation and reducing power, for eight kinds of glucose-producing 1,4-alpha-glucosyl hydrolases, including glucose-forming amylase from human urine, and alpha-glucosidases from pig serum, honey bee, buckwheat seed, rice seed, sugar beet seed, flint corn seed, and brewer's yeast. All the eight enzymes studied were found to produce alpha-glucose exclusively.
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