Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Von Ebner's gland of ferret was examined by means of light microscopy, protein, mucosubstance and enzyme histochemistry, and neurohistology. Acinar cells were replete with granules containing neutral mucosubstances and disulphides, and showed strong diffuse acid phosphatase activity and weak granular staining for peroxidase. Staining for cytochrome oxidase, succinate dehydrogenase, and NADH and NAD(P)H dehydrogenases was also seen. Basolateral plasmalemma of acinar cells showed weak, ouabain-sensitive Na+,K+-ATPase activity. Ductal cells were of a simple appearance, contained thiols and showed variable staining for acid phosphatase, dehydrogenases and cytochrome oxidase. Variable amounts of beta-glucuronidase reaction product were localized in the glandular parenchyma, being marked in atrophic areas. Prominent stellate myoepithelial cells embracing acini and also basal ductal cells were demonstrated by alkaline phosphatase. Thiamine pyrophosphatase reaction product was concentrated in blood vessels around parenchyma, with little Golgi-like staining in acinar cells. Acetylcholinesterase activity was associated with an extensive network of nerve fibres embracing parenchyma, whereas catecholamine fluorescence was not seen. The results suggest that the acini of von Ebner's gland of ferret synthesise neutral secretory glycoproteins and peroxidase. Water mobilization is inconspicuous. Lysosomal activities feature in the parenchyma, possibly a consequence of processing secretory products in acini, absorption in ducts and/or adaptation atrophy. The gland receives a rich cholinergic-type innervation, and has extensive myoepithelial and microvascular networks.
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PMID:Histochemical phenotypes of von Ebner's gland of ferret and their functional implications. 1150 41

1. Kidney homogenates from rats injected with egg white and from control rats were fractionated simultaneously into six fractions and the content of acid phosphatase, ribonuclease, desoxyribonuclease, cathepsin, and beta-glucuronidase in corresponding fractions from treated and untreated animals was compared. These observations were correlated with the amount of dark brown bottom sediments in fractions NDrI, DrII, and DrIII, and with the number of droplets in fraction NDrI. 2. It was found that after injection of egg white the amount of small droplets decreased as indicated by the decrease of the dark brown bottom layer in the sediment of fraction DrIII and by the concomitant decrease of hydrolytic enzymes in the same fraction, and that the number of large droplets increased as indicated by the increase of brown sediment in fraction NDrI and the increase in the number of droplets counted in a bacterial counting chamber in the same fraction. It was concluded that the treatment with egg white induced the transformation of small droplets into large droplets. 3. The decrease of hydrolytic enzymes in the fractions containing the small droplets was accompanied by a marked increase of these enzymes in the supernatant fluid. The enzyme content of fraction NDrI was not increased after treatment, although it contained greatly increased numbers of large droplets. Counting of the droplets in this fraction showed decreased enzymatic activity of the average large droplet after treatment with egg white. It was suggested that during the transformation of small into large droplets, a portion of the hydrolytic enzymes was released into the surrounding cytoplasm, and that this was partly responsible for the increased enzyme content of the supernatant fluid after fractionation of the kidney homogenate. In contrast to the four other hydrolytic enzymes, beta-glucuronidase was not increased in the supernatant fluid. 4. Eighteen hours after intraperitoneal injection of egg white, the specific enzymatic activities of kidney homogenates showed a 25 to 35 per cent increase for cathepsin, ribonuclease, and desoxyribonuclease, no change for acid phosphatase and beta-glucuronidase, and approximately a 7 per cent decrease for cytochrome oxidase. The increase of cathepsin, ribonuclease, and desoxyribonuclease in the total homogenate was interpreted as an indication of the formation of new enzymes, and it was suggested that this partly accounted for the increase of these enzymes in the supernatant fluid. 5. The activation of the enzymes by osmotic effects was investigated in vitro by incubation of droplet fractions in the presence of different concentrations of sucrose.
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PMID:Changes in droplet fractions from rat kidney cells after intraperitoneal injection of egg white. 1348 Oct 27

1. Nine acid hydrolases, cytochrome oxidase, alkaline phenylphosphatase and catalase were demonstrated in 0.25m-sucrose homogenates of newborn-rat calvaria. The acid hydrolases were: acid phenylphosphatase, acid beta-glycerophosphatase, beta-glucuronidase, beta-N-acetylglucosaminidase (beta-N-acetylaminodeoxyglucosidase), acid ribonuclease and acid deoxyribonuclease, showing optimum activity at about pH5; cathepsin, beta-galactosidase and hyaluronidase, with optimum activity at about pH3.6. 2. The main kinetic characters of these enzymes have been studied and methods for their quantitative assay have been worked out. The activities present in bone are given and compared with those found in liver. 3. Acid-phosphatase activity was assayed with phenyl phosphate and beta-glycerophosphate as substrates: activities with these two substrates appeared to be due to two different enzymes. Acid phenylphosphatase is particularly labile and is readily inactivated by various physical or chemical agents.
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PMID:Studies on bone enzymes. The assay of acid hydrolases and other enzymes in bone tissue. 1674 42


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