Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.13.1 (exoribonuclease)
 732 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Some biochemical characteristics of peritoneal macrophages, subcutaneous macrophages and subcutaneous cell populations containing multinucleate giant cells were compared. Subcutaneous macrophages possessed higher concentrations of succinate dehydrogenase, acid phosphatase, aryl hydroxylase, free RNase II, lecithin and free fatty acids than peritoneal macrophages, while the latter had higher concentrations of 5' -nucleotidase esterified cholesterol. These differences may be due to environmental variations depending on their anatomical position or more likely to their degree of activation. As significant numbers of multinucleate giant cells appear in the subcutaneous population the concentration aryl hydroxylase, 5' -nucleotidase lactate dehydrogenase, acid phosphatase, free ribonuclease II and esterified cholesterol falls. The concentration of succinate dehydrogenase decreases but then rises while the concentration of glucose-6-phosphate dehydrogenase increases. These highlight the differences between cell populations containing multinucleated giant cells and those composed from their precursor mononuclear phagocytes only.
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PMID:A biochemical profile of glass-adherent cell populations containing multinucleated foreign body giant cells. 78 24

Nuclei were prepared from Ehrlich ascites cells in 80% yield by homogenization of the cells in an aqueous solution containing Triton N-101 and washing of the nuclear fraction by centrifugation and resuspension. Compared to the enzyme activities present in cell extracts, approximately 47% exo-RNase I, 15% alkaline RNase II, 9% acid RNase II and 7% acid phosphatase were associated with the nuclear fraction after isolation. Exo-RNase I and alkaline RNase II were rapidly lost from nuclei during incubation at 37 degrees C. The degradation of newly synthesized RNA in nuclei incubated at 37 degrees C was followed by polyacrylamide gel electrophoresis and by characterization of acid-soluble degradation products. The rate of hydrolysis of the nuclear RNA was rapid during the initial stages of incubation and then proceeded at a much reduced rate. Nucleoside 5'-phosphates were the major acid-soluble degradation products, in agreement with the presence of exo-RNase I. Although a considerable amount of alkaline RNase II was associated with the nuclear fraction, extensive endonucleolytic cleavage of the nuclear RNA was not apparent. Compared to the processing of nuclear RNA in whole cells, however, the degradation in isolated nuclei was relatively non-specific.
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PMID:Degradation of RNA in nuclei from Ehrlich ascites cells. 109 35

The activities and androgenic regulation of seven lysosomal enzymes viz. acid phosphatase, N-acetyl hexosaminidase, alpha-mannosidase, beta-glucuronidase, DNase II, RNase II and phospholipase A was established in caput, corpus and cauda segments of monkey epididymis. Estimation of enzyme activities in the the epididymis of control, castrated and castrated-androgen replaced monkeys revealed that all the enzymes except RNase II showed higher activity in caput and corpus as compared to cauda. The enzymes were reduced markedly after castration and on subsequent androgen replacement there was a significant stimulation of the repressed activities, but the control levels were not restored. RNase II showed highest activity in cauda which was further elevated after castration. The possible role of these enzymes in sperm maturation and disposal is discussed.
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PMID:Activities and androgenic regulation of lysosomal enzymes in the epididymis of rhesus monkey. 858 24

Effect of repeated (20 days) exposure to picrotoxin (PTX) on rat liver lysosomal function was evaluated by measuring the free and total activities of acid phosphatase, cathepsin D, ribonuclease II (RNAse II) and deoxyribonuclease II (DNAse II). The free activities of the nucleases (both RNAse II and DNAse II) were increased following PTX exposure. The total DNAse II activity was increased by 2.2-fold whereas the total acid phosphatase activity was decreased by 28%. Consequently, the ratios of total activity / free activity were low in the PTX exposed groups, implying loss of membrane integrity. Cathepsin D activity was completely abolished. The results show that repeated exposure to PTX can lead to lysosomal dysfunction in liver.
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PMID:Effect of repeated intraperitoneal exposure to picrotoxin on rat liver lysosomal function. 1557 32

Effects of treatmentin vivo with the antimalarials:chloroquine (CQ), primaquine (PQ) and quinine(Q) on lysosomal enzymes and lysosomal membrane integrity were examined. Treatment with the three antimalarials showed an apparent increase in the membrane stability. CQ treatment resulted in increase in both the 'free' and 'total' activities of all the enzymes i.e. acid phosphatase, RNase II, DNase II and cathepsin D. PQ treatment lowered the 'free' and 'total' activities of acid phosphatase and cathepsin D, but the DNase II activities increased. Treatment with Q resulted in increased 'free' and 'total' activities of RNase II and DNase II. While 'free' activities of acid phosphatase and cathepsin D were low; the 'total' activities increased significantly. Our results suggest that a generalized increase in free nucleases activities following prolonged treatment with antimalarials may lead to cell damage and/or necrosis.
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PMID:Effect of antimalarials treatment on rat liver lysosomal function-Anin vivo study. 2310 85