Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.21.3 (deoxyribonuclease)
 1,528 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of eight acid hydrolases and two energy metabolism enzymes were assayed from homogenates of predominantly red (proximal heads of m. vastus lateralis, m. vastus medialis, and m. vastus intermedius) and predominantly white (distal head of m. vastus lateralis) skeletal muscle of mice belonging to one of the following groups: 1) sedentary controls, never trained or exhausted; 2) exhausted controls, exhausted once by running on a treadmill 5, 10, or 20 days before killing; 3) trained mice, exercising until killed; 4) exhausted trained mice, exercising until exhausted 5, 10 or 20 days before killing, not exercising during that period; and 5) detrained mice, terminating training 5, 10, or 20 days before killing. In untrained but not in trained animals, exhaustive exercise caused, 5 days afterward, fiber necrosis and a marked increase in the activities of beta-glucuronidase, beta-N-acetylglucosaminidase, arylsulphatase, ribonuclease, deoxyribonuclease, cathepsin D, and cathepsin C, especially in red muscle fibers. Training increased the activities of citrate synthase, beta-glucuronidase, and cathepsin D in both muscle types and those of beta-N-acetylglucosaminidase, arylsulphatase, and cathepsin C in red muscle. Effects of detraining were minor. Exhaustive exercise causes lethal and evidently also sublethal fiber injuries manifesting themselves as an activation of the lysosomal system of muscle fibers 5 days later. Training affects cellular homeostasis by causing an apparent resistance to the damaging effects of exhaustive exercise. Moderately increased hydrolase activities may reflect increased turnover in endurance-trained muscles.
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PMID:Exhaustive exercise, endurance training, and acid hydrolase activity in skeletal muscle. 22 20

Axenic Tetrahymena pyriformis, syngen 1, mating type II cells were grown in Cox's defined medium. When washed and transferred into nonnutrient dilute salt solution or resuspended in the defined medium, the intact cells secrete acid hydrolases into the medium. Cells starving in the salt solution release in 5 hr about two-thirds of their beta-glucosidase, beta-N-acetylglucosaminidase, alpha-glucosidase, and amylase activities, about one-third of their deoxyribonuclease and phosphatase activities, smaller amounts of ribonuclease, and only a negligible fraction of their proteinase activity and protein content. During this period there is practically no change in the enzyme activities (except for a sudden increase of ribonuclease activity) and protein content of cells and medium together. Cells resuspended in the nutrient medium secrete enzymes as do the starved cells, but replace this loss, so that there is a continuous increase of the activities in the total system. According to isopycnic centrifugation experiments performed in sucrose gradients, the source of the hydrolases is a special population of lysosomes which disappear from the cells during starvation. This population equilibrates in the high density region of the gradients and contains the various acid hydrolases in about the proportion in which these enzymes appear in the medium.
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PMID:Secretion of acid hydrolases and its intracellular source in Tetrahymena pyriformis. 433 53

1. Lysosome-rich fractions from rat liver were subjected to several disruptive procedures: osmotic lysis or freezing and thawing in different media, shearing forces in a high-speed blender, treatment with Triton X-100. 2. The soluble and particulate phases were then separated by high-speed centrifugation and assayed for their content of acid phosphatase, beta-galactosidase, beta-N-acetylglucosaminidase, acid proteinase, acid ribonuclease, acid deoxyribonuclease and protein. 3. The degree of elution of these hydrolases appeared to depend on both the enzyme species and the treatment. The resulting patterns of solubilization were rather complex, so that a clear-cut discrimination between soluble and structure-bound enzymes could not always be traced. 4. Although only beta-galactosidase was readily solubilizable after all treatments, acid proteinase could also be extensively eluted from the sedimentable material in the presence of EDTA and acid phosphatase was fully extracted by Triton X-100. On the other hand, considerable proportions of the other activities could not be solubilized by any of the procedures used. 5. In other experiments, the adsorbability of hydrolases on subcellular structures was investigated by measuring the partition between sedimentable particles and soluble fraction of solubilized enzymes added to ;intact' liver homogenates. 6. Large proportions of acid proteinase, ribonuclease and deoxyribonuclease, and almost all of beta-N-acetylglucosaminidase, were found to be adsorbed on the particulate material.
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PMID:Studies on the structure-bound sedimentabolity of some rat liver lysosome hydrolases. 511 7