Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C1332347 (ADH)
 2,230 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Analysis of puffing patterns in Drosophila melanogaster salivary gland chromosomes indicates the existence of a developmentally specific puff in the 35B region. This puff seems to originate from bands 35B2 or 35B3, where Adh is located, and it is expanded in more than 60% of the nuclei examined. The presence of RNA polymerase II in this puff as well as its ability to incorporate tritiated uridine shows that it corresponds to a transcriptionally active site. RNA blotting and in situ hybridization experiments indicate that Adh is transcribed, although not very actively, in salivary glands during the third larval instar. However, this tissue does not display detectable levels of ADH activity. By contrast, we have found that in midgut polytene chromosomes the 35B region is not visibly puffed in spite of the high levels of Adh transcripts detected. These results seem to suggest that puffing at the 35B region could be mainly promoted by genes closely linked to Adh, possibly with a minor contribution of this gene.
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PMID:A cytological and molecular analysis of Adh gene expression in Drosophila melanogaster polytene chromosomes. 246 76

For exploring pathogenesis of pyrimidine 5'-nucleotidase (P5'N) deficiency, a quantitative assay method for human erythrocyte pyrimidine 5'-nucleotidase was established. The specific substrate uridine monophosphate (UMP) of P5'N was used as ligand. The UPM-ADH-Sepharose 4B affinity column was prepared. P5'N of human erythrocyte was purified by ammonium sulfate fractionation and precipitation, ion chromatography and affinity chromatography. Rabbit anti-human P5'N antibody was acquired by immunizing rabbits with purified P5'N. Using rabbit anti-human antibody as the coated anti-body and HRP-rabbit anti-human antibody as demonstrated anti-body, the double antitody sandwich ELISA for quantitative assay of human erythrocyte P5'N was established after square rank trial, antigen blocked trial and antigen substituted test. Results showed that the titer of rabbit anti-human erythrocyte was 1:4 and the sensitivity of double antibody sandwich ELISA was 5 ng/ml. Its blocking rate was more than 95% and the rate of substitution less than 30%. The content of P5'N was (71.77 + 10.98) ng/mg NHP in normal human erythrocyte. A new ELISA method for quantitative determination of human erythrocyte P5'N was first established. It not only had high specificity and sensitivity but also could assay the minimun content of P5'N as 5 - 20 ng/ml. It could be a suitable method for large sample in clinics.
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PMID:[Establishment of Quantitative Assay for Human Erythrocyte Pyrimidine 5'-Nucleotidase Content by Double Antibody Sandwich ELISA] 1257 82