Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Drug
Enzyme
Compound
Query: EC:3.2.1.21 (
beta-glucosidase
)
3,280
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The effect of Fusarium sporotrichiella v. sporotrichioides mycotoxin (sporofusarin) on the total and non-sedimentary supernatant activity of 13 marker-enzymes of subcellular particles (2 mitochondrial enzymes-cytochrome oxidase and malate dehydrogenase; 8 lysosomal enzymes -- acid phosphatase, acid RNAase, acid DNAase, arylsulphatases A and B, beta-N-acetylglucosaminidase, beta-glucuronidase, beta-galactosidase and
beta-glucosidase
; 2 microsomal enzymes -- glucose-6-phosphatase and
acetylesterase
; plasma membrane enzyme -- alkaline phosphatase) of the rat liver, kidney, spleen and bone-marrow was studied in in vivo experiments. The latter demonstrated that sporofusarin effects were characterized by a significant organ and organella specificity, viz. the toxin caused a sharply increased activity, mainly of lysosomes enzymes and labilization of the lysosomal membranes, primarily in the spleen and the bone-marrow. A conclusion is drawn that the discovered selective destructive action of sporofusarin on the lysosomes may be regarded as a new phenomenon that, possibly is directly related to the characterization of the mechanism responsible for a specific effect produced by sporofusarin.
...
PMID:[Lysosomal component in the mechanism of the toxic effect of sporofusarin]. 94 27
Effect of ethanol on functional activity of isolated perfused rat liver was studied (rate of O2 utilization, absorption of bromosulpholeine from perfusate, bile formation); total activity and activity in supernatant of nine marker enzymes were also determined (malate dehydrogenase, beta-glucuronidase, arylsulphatases A and B, beta-galactosidase,
beta-glucosidase
,
acetylesterase
, glucoso-6-phosphatase, alanine aminotransferase and aspartate aminotransferase). Activity of the enzymes was simultaneously studied in perfusate. Ethanol (0.5%) caused distinct impairement in functional activity of isolated liver; rate of bile formation and absorption of bromosulpholeine from perfusate were primarily altered. Degree of impairements in functional activity of liver tissue correlated with the concentration of ethanol in perfusate. In analysis of correlation between the total activity of the enzymes in liver tissue and their activity in supernatants and perfusate it was shown that the concentration (1%) of ethanol used did not produce damaye effect on plasma membranes and membranes of subcellular structures of hepatocytes, but, within certain limits, it displayed a stabilizing effect.
...
PMID:[Effect of ethanol on stability of cell membranes in experiments using isolated liver]. 121 Jan 8
The outer membrane (OM) of Fibrobacter succinogenes was isolated by a combination of salt, sucrose, and water washes from whole cells grown on either glucose or cellulose. The cytoplasmic membrane (CM) was isolated from OM-depleted cells after disruption with a French press. The OM and membrane vesicles isolated from the extracellular culture fluid of cellulose-grown cells had a higher density, much lower succinate dehydrogenase activity, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis protein profiles different from those of the CM. The OM from both glucose- and cellulose-grown cells and the extracellular membrane vesicles from cellulose-grown cultures exhibited higher endoglucanase, xylanase, and
acetylesterase
activities than the CM and other cell fractions. Endoglucanase 2 was absent from the isolated OM fractions of glucose- and cellulose-grown cells and from the extracellular membrane vesicles of cellulose-grown cells but was present in the CM and intracellular glycogen granule fractions, while endoglucanase 3 was enriched in the OM. Cellobiosidase was located primarily in the periplasm as previously reported, while
cellobiase
was mainly present in the glycogen granule fraction of glucose-grown cells and in a nongranular glycogen and CM complex in cellulose-grown cells. The
cellobiase
was not eluted from glycogen granules by cellobiose, maltose, and maltotriose nor from either the granules or the cell membranes by nondenaturing detergents but was eluted from both glycogen granules and cell membranes by high concentrations of salts. The eluted
cellobiase
rebound almost quantitatively when diluted and mixed with purified glycogen granules but exhibited a low affinity for Avicel cellulose. Thus, we have documented a method for isolation of OM from F. succinogenes, identified the OM origin of the extracellular membrane vesicles, and located glycanases and
cellobiase
in membrane and glycogen fractions.
...
PMID:Separation of outer and cytoplasmic membranes of Fibrobacter succinogenes and membrane and glycogen granule locations of glycanases and cellobiase. 822 22
Beta-D-Glucopyranosidase (betaG,
EC 3.2.1.21
) has been isolated from some collateral activities, alpha-L-arabinofuranosidase (Ara, EC 3.2.1.55), alpha-L-rhamnopyranosidase (Rha, EC 3.2.1.40), and o-
acetylesterase
(Est, EC 3.1.1.53), using a commercial enzyme preparation and a simple method economically sustainable for the food industry. The procedure comprises precipitation of extraneous substances by adding ethanol and CaCl2, ultrafiltration, and adsorption, first on bentonite and then on chitosan. The results obtained were the complete isolation of betaG from the above-mentioned activities, a drastic reduction in extraneous compounds, such as brown substances and polysaccharides, and a slight increase in purification.
...
PMID:Inexpensive isolation of beta-D-glucopyranosidase from alpha-L-arabinofuranosidase, alpha-L-rhamnopyranosidase, and o-acetylesterase. 1200 63