Amphibian eggs and embryos as well as mammalian cells have been reported to contain an activity that unwinds double-stranded RNA. We have now found that adenosine residues have been modified in the RNA products of this unwinding activity. Although the modified RNA remains double-stranded, the modification causes the RNA to be susceptible to single-strand-specific RNase and to migrate as a retarded smear on a native polyacrylamide electrophoresis gel. The modification is specific for double-stranded RNA. At least 40% of the adenosine residues can be modified in vitro in a given random sequence RNA molecule. By using standard twodimensional TLC and HPLC analyses, the modified base has been identified as inosine. Mismatched base-pairing between inosine and uridine appears to be responsible for the observed characteristics of the unwound RNA. The biological significance of this modifying activity and also of the modified double-stranded RNA is discussed.Recently the detection of a double-stranded RNA (dsRNA) unwinding activity in mammalian cells and amphibian eggs was reported (1-3). The unwinding activity has been analyzed by an in vitro assay system using crude cell extracts and duplex RNA formed by sense and antisense complementary RNA strands (1, 3). After incubating the duplex RNA with the cell extract, the unwound RNA is detected both by its retarded smear on a native polyacrylamide gel and by its sensitivity to single-strand-specific RNase. The unwinding activity is abolished by proteinase treatment, suggesting that a protein is involved, and appears not to require ATP. The activity is specific for dsRNA: it is inhibited by preincubation of the reaction mixture with a 50-fold molar excess of dsRNA but not by single-stranded RNA, double-stranded DNA, single-stranded DNA, or tRNA (1, 3). The unwinding activity seems not to have sequence specificity: it unwinds different types of dsRNA formed in vitro from sense and antisense RNAs of l3-globin, c-myc, and chloramphenicol acetyltransferase (1-3). The unwinding activity is low in quiescent mouse fibroblast 3T3 cells but increases when the cells are stimulated to renew growth by serum, suggesting that it may be regulated in a cell-cycle-dependent manner (3).In our previous report, we noted several odd characteristics of the unwound RNA. The dsRNA is never completely dissociated to monomer form even by including excess protein, longer incubation times, or additional fresh protein added to previously unwound RNA for an extended length of time (3). If the unwound RNA is heated to 90°C in 90% formamide, however, it is fully denatured into full-length monomer form. In addition, the unwound RNA does not hybridize back to its native state when allowed to reanneal in the hybridization conditions used originally to form the duplex. These puzzling observations led us to infer that the unwound RNA was not completely denatured but was somehow modified to a form that was incapable of complete rehybridization (3).In the present study these findings are extended to demons...
Three experiments, using 344 pigs, were conducted to evaluate the influence of beta-glucan on growth performance, neutrophil and macrophage function, haptoglobin production, and resistance to Streptococcus suis challenge in weanling pigs. In Exp. 1, 144 pigs were used to evaluate the influence of .1% dietary beta-glucan in a soybean meal- or milk protein-based diet on growth performance and neutrophil function. Pigs fed beta-glucan from d 7 to 14 after weaning had lower ADFI (P < .01) and, although not significant, ADG was lower for pigs fed beta-glucan than for pigs fed control diets. However, no differences were observed in growth performance or neutrophil function for pigs fed control or diets containing beta-glucan from d 7 to 35 after weaning. Experiment 2 was a 28-d growth assay in which pigs were fed a diet with or without .1% beta-glucan, containing 7.5% spray-dried plasma protein and 25% dried whey from d 0 to 14 after weaning. Pigs then were fed corn-soybean mealbased diets containing 2.5% spray-dried blood meal and 10% dried whey. No differences in growth performance were observed. Experiment 3 was a 35-d assay to evaluate growth performance, neutrophil and macrophage function, and plasma haptoglobin concentration. Pigs were challenged on d 28 postweaning with intravenous S. suis. In Exp. 3, pigs were fed diets without or with .025 or .05% beta-glucan. Dietary beta-glucan did not influence neutrophil or macrophage function. However, pigs fed diets containing .025% beta-glucan had increased (P < .05) ADG and ADFI and were heavier (P < .05) on d 28 after weaning than pigs fed the control diet. No differences in feed efficiency (G/F) were detected between treatments. Pigs fed beta-glucan had decreased (P < .10) plasma haptoglobin on d 14, 21, and 28 after weaning. However, Fisher's Exact test revealed that more (P < .04) pigs fed a diet containing .025% beta-glucan died by d 12 after challenge with S. suis. In conclusion, these data suggest the existence of a complex interaction involving growth performance and resistance to S. suis in pigs fed .025% beta-glucan.
Men (N = 526) who patronized gay bars in three cities completed measures of sexual behavior covering the previous 3 months and psychological measures theoretically pertinent to AIDS risk. Thirty-seven percent of the sample reported engaging in unprotected anal intercourse, the behavior most strongly associated with transmission of human immunodeficiency virus (HIV) infection. Perceived peer norms concerning the acceptability of safer sex practices, AIDS health locus of control scores, risk behavior knowledge, age, and accuracy of personal risk estimation, but not personal HIV serostatus knowledge, were associated with high-risk and precaution-taking behavior.
Blood group incompatibility causes transfusion reactions and neonatal isoerythrolysis in cats. We investigated the molecular nature of the blood group antigens from cats that had blood type A, B, and AB erythrocytes. Naturally occurring anti-type B antibodies, Triticum vulgaris lectin, monoclonal antibody (MoAb) 32–27, and MoAb R-24 were used in agglutination tests, Western blots, and thin-layer chromatography (TLC) enzyme immunostaining. Type A erythrocytes had NeuGc-NeuGc-Galactose-Glucose-Ceramide ([NeuGc]2GD3) where NeuGc represents N-glycolylneuraminic acid, and NeuAc-NeuGc-GD3, where NeuAc represents N-acetylneuraminic acid, and may have [NeuGc]2 disialylparagloboside and NeuAc-NeuGc-disialylparagloboside. Type B erythrocytes only had [NeuAc]2GD3. Type AB erythrocytes had [NeuGc]2GD3, NeuAc-NeuGc-GD3, and [NeuAc]2GD3. Blood group antigens were also found on a 50-Kd membrane protein. We conclude that type B erythrocytes are characterized by [NeuAc]2GD3 as the only form of this ganglioside and the presence of NeuAc on a 50-Kd membrane protein. NeuGc is the major determinant of the A antigen; specifically, [NeuGc]2GD3 is the major glycolipid form. The A antigen is also present on a 50-Kd membrane protein.
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