Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Activities of several hydrolases were studied in blood serum, synovial fluid and musculus femoris of rats with adjuvant arthritis. Alterations in activity of some hydrolases in blood serum were investigated after treatment of animals with nonsteroid antiinflammatory drugs (indometacin, aspirin, bruphene), prednisolone or after the treatment with immunodepressants (imurane, D-penicillamine) and theophylline. Distinct activation of several lysosomal enzymes was observed in rats with arthritis: acidic cathepsins and beta-D-glucuronidase--in all the samples studied; beta-D-galactosidase--in synovial fluid and musculus femoris; hyaluronidase--in synovial fluid and blood serum as well as alpha-D-galactosidase and arylsulfatases (A + B)--in the latter. Activation of these enzymes was accompanied by a decrease in activity of other hydrolases: beta-D-glucosidase, hyaluronidase and alpha-D-galactosidase--in musculus femoris; alpha-D- and beta-D-glucosidases--in blood serum. In treatment of the impaired rats aspirin was the most effective drug, bruphene was less effective. Only theophylline among the drugs studied activated distinctly alpha-D-glucosidase in blood serum. Combination of nonsteroid antiinflammatory drugs (like aspirin and bruphene) with theophylline was apparently the most suitable way for treatment of arthritis under the experimental conditions.
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PMID:[Hydrolytic enzymes in biological fluids and skeletal muscle of rats with adjuvant arthritis]. 66 68

Tissues of rats with adjuvant arthritis manifested differences in activity and distribution between free, latent and membrane-bound forms of acid catepsins, alpha-D- and beta-D-galactosidases, alpha-D- and beta-D-glucosidases, beta-D-glucorunidase, hyaluronidase, acid phosphatase, arylsulphatases (A+B). Activation of certain hydrolytic enzymes is observed in tissues of the liver, kidneys, heart and spleen: a rise in total activity (of arylsulphatase in the liver and acid catepsins in the spleen; hyaluronidase in the kidneys, beta-D-glucuronidase in the heart) and a change in the ratio of different forms with a simultaneous increase in the activity of free form (of hyaluronidase in the spleen, acid phosphatase in the heart and liver). Inhibition of alpha-D-glucosidase in the liver and beta-D-glucosidase in the spleen is also detected. A decrease in the activity of beta-D-glucuronidase in the spleen is pronounced in a significant decrease in the activity of each enzyme free form with no changes in the total activity.
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PMID:[Hydrolytic enzymes of rat tissues with adjuvant arthritis]. 72 90

The lysosomal glycosidase activity of the eye tissues (the sclera and cornea), the bone tissues and cartilage were studied. The intraperitoneal injection of tyrocalcitonine (TCT), deoxycorticosterone (DOCS), hydrocortisone (HC), and somatotropic hormone (STH) influenced both the activity of beta-galactosidase, beta-glucosidase, and hyaluronidase, the the functional state of thy lysosomal membranes of the connective tissues under investigation. GC and STH caused stabilization, whereas DOCS and large doses of TCT--a labilizing effect on the lysosomal membranes and tissues understudy. The absolute activity of the enzymes in the homogenates decreased after the HC and STH injection. DOCS produced an opposite effect.
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PMID:[Responses of different types of connective tissue to hormone administration]. 89 Jan 33

Biochemical study of the activity of the enzyme systems of different localization in the cell connected with the subcellular structures - lysosomes (hyaluronidase, N-acetyl-beta-D-glucosaminidase, beta-glucosidase) and hyaloplasm-soluble (aldolase of neuraminic acid), and also a study of the state of the enzyme-substrate groups, belonging to the immunoreactive biopolymeres containing a carbohydrate (glucoproteins, glycosaminoglycanes) was carried out in the tissues of different organs (the liver, kidneys, small intestine, skin) and in the blood serum of albino rats exposed to the isolated and joint (in combination with various doses of ultraviolet irradiation) action of the chemical allergen (dinitrochlorbenzene). General and specific regularities of metabolic reactions, the appearance of which could presumably be connected with the development of delayed allergy were revealed.
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PMID:[Study of metabolic mechanisms of the isolated and combined effect of a chemical allergen]. 102 7

The authors present the results of study or fegularities attending the changes in the activity of free, total and bound fractions of the lysosomal enzymes--beta-glucosidase and beta-galactosidase in the thymus and the spleen of rabbits under conditions of DOCA administration. The activity of the enzymes was studied 30 min, 1, 4, 12, 24 and 48 hours after a single injection of the hormone. DOCA administration caused biphasic changes in the activity of both glycosidases. A marked increase in the activity of all the enzyme fractions during the first experimental hours was later replaced by their fall. An increase in the activity of glycosidases at the early periods of DOCA administration pointed to the intensification of the enzymatic synthesis, and also could be associated with the spicific induction of the enzymatic activity. The activity of beta-glucosidase and of beta-galactosidase directly depended on DOCA dose. Effects similar to the experiments in vivo were obtained in vitro. The activity of hyaluronidase under the effect of Dca decreased considerably in the thymus and the spleen, particularly at the early experimental periods, pointing to reduction of tissue permeability of the lymphoid organs.
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PMID:[The effect of desoxycorticosterone acetate on the activity of the lysosomal enzymes of lymphoid organs]. 113 80

The serum concentrations of FSH, LH, prolactin, testosterone, and estradiol and the enzymatic activities of hyaluronidase, glucosidases (alpha-glucosidase, beta-glucosidase, alpha-mannosidase, N-acetyl-beta-D-glucosaminidase, beta-glucuronidase, and beta-galactosidase), lactate dehydrogenase and its isoenzymes (LDH1, LDH2, LDH3, LDH-X, LDH4), and total proteins were measured in the semen of 69 subjects (8 normozoospermic controls, 7 secretory, and 54 excretory azoospermic subjects). FSH levels rose with the deterioration in spermatogenesis and served to differentiate the secretory from the excretory azoospermias. The only source of hyaluronidase and LDH-X in the ejaculate is the spermatozoa. alpha-Glucosidase activity essentially originates in the epididymis. The seminal determination of alpha-glucosidase and, to a lesser extent, alpha-mannosidase and N-acetyl-beta-D-glucosaminidase helps rapidly, sensitivity, reliably, and noninvasively to differentiate secretory azoospermias (with higher enzymatic activity) from the excretory type (less enzymatic activity) and may be of use in identifying with a certain degree of reliability the site of obstruction in the male genital tract.
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PMID:Enzyme and hormonal markers in the differential diagnosis of human azoospermia. 153 Mar 67

Previous studies have shown that bovine retinas incubated with [3H]galactose incorporated it, unmodified, into large molecules. Light and electron microscope autoradiography showed a significant proportion of the label to be in cone inner segments, and pulse-chase studies showed it was subsequently transported to the synaptic pedicles. In this report, evidence is presented to show that the galactose-labelled macromolecules are resistant to hydrolysis by proteolytic enzymes, testicular hyaluronidase, chondroitinase ABC, beta-glucosidase and beta-glucuronidase, but are readily degraded by alpha-amylase and beta-galactosidase, and to a lesser extent by beta-amylase. Treatment with alpha-amylase also leads to specific removal of radioactivity from cone inner segments and pedicles, as judged by light-microscopic autoradiography. These studies appear to indicate that the cone-specific galactose label is in glycogen or glycogen-like molecules.
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PMID:D-[3H]galactose incorporation into glycogen in retinal cone cells. 231 72

A biochemical scheme was developed by which strains of Streptococcus constellatus, Streptococcus intermedius, and Streptococcus anginosus can reliably be distinguished from within the "Streptococcus milleri group." Strains identified as S. intermedius were differentiated by the ability to produce detectable levels of alpha-glucosidase, beta-galactosidase, beta-D-fucosidase, beta-N-acetylgalactosaminidase, beta-N-acetylglucosaminidase, and sialidase with 4-methylumbelliferyl-linked fluorogenic substrates in microdilution trays after 3 h of incubation at 37 degrees C, together with the production of hyaluronidase. Strains of S. constellatus and S. anginosus were differentiated by the production of alpha-glucosidase and hyaluronidase by the former and the production of beta-glucosidase by the latter. The majority of strains of the S. milleri group obtained from dental plaque were identified as S. intermedius, as were most strains isolated from abscesses of the brain and liver. Strains of S. constellatus and S. anginosus were from a wider variety of infections, both oral and nonoral, than were strains of S. intermedius, with the majority of strains from urogenital infections being identified as S. anginosus.
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PMID:Phenotypic differentiation of Streptococcus intermedius, Streptococcus constellatus, and Streptococcus anginosus strains within the "Streptococcus milleri group". 238 Mar 75

Smooth muscle cells were dissociated from normal rabbit aorta by incubating the tissue in Hanks' solution containing elastase, collagenase, and hyaluronidase. The isolated cells contained significant amounts of the following acid hydrolases: N-acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, beta-glucosidase, acid phosphatase, and cathepsins C and D. The cells were disrupted and fractionated by isopycnic centrifugation on sucrose density gradients in the Beaufay automatic zonal rotor. Lysosomes with a modal density of 1.16 were identified by the distribution of these acid hydrolases and by the latency of N-acetyl-beta-glucosaminidase and beta-galactosidase. Other particulate enzymes studied in these sucrose gradients included cytochrome oxidase and monoamine oxidase (mitochondria), 5'-nucleotidase and leucyl-beta-naphthylamidase (plasma membrane), and catalase (? peroxisome). This microanalytical subcellular fractionation technique is applicable to the study of milligram quantities of many other tissues, both normal and pathological.
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PMID:Lysosomes of the arterial wall. I. Isolation and subcellular fractionation of cells from normal rabbit aorta. 434 42

The effect of in vitro capacitation (events that occur before the acrosome reaction) on the acrosomal enzymes of human spermatozoa was determined. Capacitation of human spermatozoa was assessed by their ability to penetrate denuded hamster oocytes. The activities of a number of enzymes commonly associated with the sperm acrosome, including nonzymogen acrosin, proacrosin, inhibitor-bound acrosin, hyaluronidase, acid phosphatase, beta-glucuronidase, beta-glucosidase, beta-N-acetylglucosaminidase, beta-galactosidase and beta-N-acetylgalactosaminidase were assessed. With the exception of acid phosphatase, no alteration in enzyme activity occurred after 4 h of incubating the spermatozoa under capacitation conditions although gamete fusion took place. The acid phosphatase levels decreased twofold, presumably due to the loss of seminal (prostatic acid phosphatase that loosely adheres to spermatozoa. After 8 h of capacitation, a large decrease in sperm enzyme levels took place only in the case of hyaluronidase, although small decreases were also noted in total acrosin, proacrosin and inhibited acrosin. No new electrophoretically migrating forms of acrosin were observed. Decreases in total acrosin and proacrosin, but not in inhibited acrosin, also occurred when spermatozoa were incubated under noncapacitating conditions for 8 h, indicating that capacitation may specifically cause the release of some acrosin inhibitor from human spermatozoa. It is concluded that, with the possible exception of hyaluronidase, the in vitro capacitation of human spermatozoa does not cause a major change in its acrosomal enzyme content so that these hydrolases are fully present before the acrosome reaction takes place during gamete fusion. Serum albumin appears to protect against the loss of some of these enzymes since the activity of several glycosidases was significantly reduced when the spermatozoa were incubated for 8 h in human serum albumin-free medium.
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PMID:Acrosomal enzymes of human spermatozoa before and after in vitro capacitation. 640 71


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