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Thin Co/Pd multilayers, with room temperature perpendicular anisotropy and an enhanced surface scattering, were studied for the possible use in the extraordinary Hall effect (EHE) - based magnetic memory devices. Polarity of the EHE signal was found to change from negative in thick samples to positive in thin ones. Reversal of EHE sign was also observed in thick samples with aging. The effect is argued to be related to the dominance of surface scattering having the EHE polarity opposite to that of the bulk.
We report that protease nexin-1 (PN-1), a serine protease inhibitor known to have neurite-promoting effects, is made by Schwann cells in tissue culture. Three modalities have been used to demonstrate the presence of PN-1 in Schwann cell cultures. Immunostaining of the cultures with anti-PN-1 antibody gives positive staining over cells and matrix. Western blots of Schwann cell conditioned medium (CM) using anti-PN-1 antibody show a band that co-migrates with the PN-1 standard at 45 kDa. Biochemical assay for protease inhibitory activity shows that CM inhibits thrombin activity in a calorimetric assay. The CM-mediated inhibition of thrombin is reversed if the CM is pre-incubated with anti-PN-1 antibody.
A major impediment to successful implementation of gene therapy for treatment of muscular dystrophy is the restricted infectivity of mature muscle fibers with viral vectors. This phenomenon has been observed with adenovirus vectors and more recently with herpes simplex virus type 1 (HSV-1)-based vectors. Here we report findings of morphological studies designed to experimentally determine the mechanism underlying the rapid reduction in vector-mediated gene delivery concomitant with the maturation of muscle fibers. Using immunohistochemistry and confocal microscopy, we have colocalized HSV-1 and collagen IV, a major component of the basal lamina, in HSV-1-injected muscles and determined that the virus penetrates and expresses a transgene (lacZ) in muscle fibers of newborn animals but cannot efficiently penetrate adult myofibers. This wa...
Inherited defects in the gene for methylmalonyl-CoA mutase (EC 5.4.99.2) result in the mut forms of methylmalonic aciduria. mut- mutations lead to the absence of detectable mutase activity and are not corrected by excess cobalamin, whereas mut- mutations exhibit residual activity when exposed to excess cobalamin. Many of the mutations that cause methylmalonic aciduria in humans affect residues in the C-terminal region of the methylmalonyl-CoA mutase. This portion of the methylmalonyl-CoA mutase sequence can be aligned with regions in other B12 (cobalamin)-dependent enzymes, including the C-terminal portion of the cobalamin-binding region of methionine synthase. The alignments allow the mutations of human methylmalonyl-CoA mutase to be mapped onto the structure of the cobalamin-binding fragment of methionine synthase from Escherichia co...
Methionine synthase catalyzes the remethylation of homocysteine to methionine via a reaction in which methylcobalamin serves as an intermediate methyl carrier. Over time, the cob(I)alamin cofactor of methionine synthase becomes oxidized to cob(II)alamin rendering the enzyme inactive. Regeneration of functional enzyme requires reductive methylation via a reaction in which S-adenosylmethionine is utilized as a methyl donor. Patients of the cblE complementation group of disorders of folate/cobalamin metabolism who are defective in reductive activation of methionine synthase exhibit megaloblastic anemia, developmental delay, hyperhomocysteinemia, and hypomethioninemia. Using consensus sequences to predicted binding sites for FMN, FAD, and NADPH, we have cloned a cDNA corresponding to the “methionine synthase reductase” reducing system requ...
Positive association between obesity and survival after breast cancer was demonstrated in previous meta-analyses of published data, but only the results for the comparison of obese versus non-obese was summarised.
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