Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

The activity of the membrane-bound enzymes of the microvillous zone of the entreocytes (maltase, sucrase, trehalase, lactase, cellobiase, alkaline phosphatase and leucylaminopeptidase) was studied in mucosal smears from the proximal jejunum, ileum, caecum and sigmoid flexure in a group of control (C) (8) and germ-free (GF) (7) rabbits. The trypsin and chymotrypsin activity of the contents of the ileum, caecum and sigmoid flexure was studied in 6 C, 5 GF and 5 monocontaminated (MC) rabbits. In summing up it can be stated that the individual membrane-bound enzymes have a different gradient in the various intestinal segments of C and GF rabbits and that they differ reciprocally in character. The maximum statistically significant differences between GF and C rabbits were found in the ileum; in the jejunum they were somewhat smaller and in the caecum smaller still (in this localization the difference was C versus GF). Striking differences in the proportion of the individual disaccharidases were found inthe jejunum and ileum of C rabbits compared with GF rabbits, in which, in both these segments of small intestine the relationship maltase greater than sucrase greater than trehalase greater than lactase was preserved. The proteolytic activity of the intestinal contents likewise had a different gradient character in C, MC and GF rabbits. The maximum activities (especially trypsin) were found in MC animals. The microbial flora is one of the factors regulating the enzymatic activities of the microvillous zone of the enterocytes and it also significantly influences the proteolytic activity of the intestinal contents. This influence is particularly marked in the distal part of the alimentary tube.
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PMID:Digestive enzymes of the mucosa of the small intestine and trypsin and chymotrypsin proteolytic activity of the intestinal contents of germ-free, monocontaminated and conventional rabbits. 35 55

The enzymatic activities of 53 strains of Pseudomonas cepacia were determined by using the API ZYM system. Strong alkaline phosphatase, acid phosphatase, butyrate esterase, caprylate esterase, myristate lipase, leucine arylamidase, and phosphoamidase activities were consistently detected in all strains. Weak activities were observed for valine arylamidase, beta-glucosidase, and N-acetyl-beta-glucosaminidase. No activities could be demonstrated for cystine arylamidase, trypsin, chymotrypsin, alpha-galactosidase, beta-galactosidase, beta-glucuronidase, alpha-glucosidase, alpha-mannosidase, and alpha-fucosidase. Enzymatic activities of pseudomonads may provide useful information about their pathogenesis and information for identification of Pseudomonas species.
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PMID:Enzymatic characterization of Pseudomonas cepacia by API ZYM profile. 335 98

The effects of exogenously added phospholipase A2 (PLA2) and its hydrolytic products in isolated bullfrog sciatic nerve were investigated. Nerves were pretreated for 3 h with a dose of trypsin which did not affect conduction in order to enhance penetration of the added agents. Treatment of nerves with beta-glucosidase, neuraminidase or chymotrypsin had no effect on conduction. Whereas incubation of the nerves with normal Ringers for 2 h had no significant effect on conduction, incubation with PLA2 in Ringers caused decrements in the height of the compound action potential in a dose-related manner. In addition, incubation of the nerves with 10 mg/ml lysolecithin, arachidonic acid, or docosahexaenoic acid caused marked decrements in the height of the compound action potential. Electron microscopic analysis of nerves after each treatment which caused conduction block revealed varying levels of myelin damage. Although myelin was damaged at the paranodal and/or internodal region, depending on the agents used, the axonal membrane appeared to be intact at the ultrastructural level. It was concluded that the block in conduction resulting from PLA2 was due to the formation of lysolecithin and long chain polyunsaturated fatty acids.
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PMID:Mechanism of phospholipase A2-induced conduction block in bullfrog sciatic nerve. I. Electrophysiology and morphology. 348 69

Extraction of control human spleen glucocerebrosidase with sodium cholate and butan-l-ol reversibly inactivates the enzyme in terms of its ability to hydrolyse the water-soluble substrate 4-methylumbelliferyl beta-D-glucopyranoside (MUGlc). The acidic brain lipid galactocerebroside 3-sulphate (sulphatide) reconstitutes beta-glucosidase activity in a strongly concentration-dependent manner. In this study we show that sulphatide exhibits three critical micellar concentrations (CMCs): CMC1, 3.72 microM; CMC2, 22.6 microM; CMC3, 60.7 microM. We designate the aggregates formed at these CMCs as primary, secondary and tertiary micelles respectively. From the results of kinetic studies performed at various sulphatide concentrations (0.012-248 microM), we found that sulphatide monomers (less than 3 microM) decreased the Km (for MUGlc) of control glucocerebrosidase from 11 to 4.6 mM, and lowered the Vmax. 2-fold. However, secondary and tertiary micelles were required for expression of high control glucocerebrosidase activities. Glucocerebrosidase prepared from the spleen of a patient with non-neuronopathic type 1 Gaucher's disease exhibited a very low Km (2.8 mM) even in the absence of exogenous lipid, and sulphatide monomers had no effect on the mutant enzyme's Km or Vmax. However, secondary or tertiary micelles markedly increased the Vmax. of the type 1 glucocerebrosidase to 60% of the corresponding control enzyme value. In contrast, for the glucocerebrosidase of the neuronopathic type 2 case, although sulphatide decreased the Km from 9.2 to 1.7 mM, the Vmax. never reached more than 5% that of the control enzyme, even at high concentrations of sulphatide. In addition, we found that secondary and tertiary sulphatide micelles enhanced the rate of inactivation of all three glucocerebrosidase preparations by chymotrypsin. Collectively, these results indicate the presence of two sulphatide-binding sites on glucocerebrosidase: one that enhances substrate binding, and another that enhances catalysis.
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PMID:A kinetic study of the effects of galactocerebroside 3-sulphate on human spleen glucocerebrosidase. Evidence for two activator-binding sites. 380 Sep 8

Enzymatic characterization of 48 Aeromonas hydrophila complex isolates from various sources was determined with the API ZYM system (Analytab Products, Plainview, N.Y.). All isolates lacked valine and cystine aminopeptidases, chymotrypsin, alpha-mannosidase, alpha-fucosidase, alpha-galactosidase, and beta-glucuronidase but possessed caprylate esterase-lipase, leucine aminopeptidase, acid phosphatase, phosphoamidase, and N-acetyl-beta-glucosidase. Variability was found in the presence of alkaline phosphatase, butyrate esterase, myristate lipase, trypsin, beta-galactosidase, alpha-glucosidase, and beta-glucosidase. No significant differences were evident among the enzymatic profiles of isolates from various sources.
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PMID:Enzymatic characterization of Aeromonas hydrophila complex by the API ZYM system. 681 46

An epidemiologic study of Pasteurella haemolytica serovar 1 (Ph1) in market-stressed feeder calves from 7 farms in eastern Tennessee was conducted. The nasal mucus of each calf was cultured sequentially at the farm of origin (day 0), at an auction market (day 133), and at a feedyard in Texas (days 141, 148, 155, and 169). Of the 103 calves tested, 77 were culture-positive, including 1 on day 0, 1 on day 133, 20 on day 141, 57 on day 148, 50 on day 155, and 14 on day 169. From the 143 Ph1 isolates, 20 enzyme profiles were determined by use of a commercial enzyme system that detects 19 enzymatic reactions; 4 antimicrobial susceptibility profiles were obtained, using the disk-diffusion method, which evaluated susceptibility to 11 antibacterial drugs. All isolates were positive for acid phosphatase and alkaline phosphatase, but were negative for alpha-galactosidase, alpha-mannosidase, beta-glucosidase, beta-glucuronidase, cystine aminopeptidase, N-acetyl-beta-glucosaminidase, and trypsin. Other positive enzyme reactions included: leucine aminopeptidase, 140 Ph1 isolates; phosphohydrolase, 90 isolates; alpha-fucosidase, 63 isolates; esterase (C4), 59 isolates; valine aminopeptidase, 30 isolates; esterase lipase (C8), 24 isolates; beta-galactosidase, 2 isolates; and alpha-glucosidase, chymotrypsin and lipase (C14), 1 isolate each. Thirty-four Ph1 profiles were identified, using combined enzyme and antimicrobial susceptibility profiles. The data indicate that the strains isolated during the feedyard period may have been determined more by farm of origin (P < or = 0.001) than by habitation with calves from other farms while in the feedyard.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Identification of Pasteurella haemolytica A1 isolates from market-stressed feeder calves by use of enzyme and antimicrobial susceptibility profiles. 842 78

Membranes were prepared from tissues of the carp Ctenopharynogodon idellus including liver, kidney, intestine, adipose tissue, ovary, gill, heart, muscle and spleen. The carp liver and intestine membranes bound 125I-labeled bovine growth hormone and the binding could be displaced by cold bovine growth hormone. No changes in the ability to bind 125I-labeled bovine growth hormone occurred after treatment of the carp liver membrane with DNase, RNase, alpha-amylase and beta-glucosidase, suggesting that neither nucleic acids nor carbohydrates played an important part in the hepatic binding of growth hormone. Treatment of carp liver membranes with either chymotrypsin or trypsin produced a decrease in the growth hormone binding activity, indicating that the growth hormone receptor on carp liver membrane is a protein. Treatment of carp liver membranes with p-chloromercuribenzoate brought about a reduction in 125I-bGH binding. The inhibition could be reversed by dithioerythritol, suggesting the involvement of essential sulfhydryl group in bGH binding.
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PMID:Presence of growth hormone receptors in carp liver and intestine. 849 May 77

The enzymatic activity of 70 feline and canine Microsporum canis isolates was determined by the Api-Zym test. The liquid phase of cultures, inoculated into Tryptic Soy Broth, was used to examine 19 enzymes. Considerable differences were observed among the extracellular enzymatic patterns. All the isolates produced alkaline phosphatase and beta-glucosidase, while lipase (C14), trypsin, chymotrypsin, beta-glucuronidase, and alpha-fucosidase activity was never revealed. Esterase (C4) activity was present in 57 samples (81%), esterase lipase (C8) in 31 (44%), leucine arylamidase in 35 (50%), valine arylamidase and cystine arylamidase in 7 (10%), acid phosphatase in 64 (91%), naphthol-AS-BI-phosphohydrolase in 60 (86%), alpha-galactosidase in 5 (7%), beta-galactosidase in 6 (8%), alpha-glucosidase in 25 (36%), N-acetyl-beta-glucosaminidase in 41 (58%), and alpha-mannosidase in 51 (73%). The beta-galactosidase activity of M. canis has not been reported previously. Remarkable variations of intensity for each enzymatic activity were also detected. It is believed that these results could provide basic data for further investigations on the pathogenic role of enzymes secreted by M. canis.
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PMID:Extracellular enzymatic activity of Microsporum canis isolates. 868 26

Structures of the N-linked oligosaccharide attached to the heavy chain of a heterologous murine IgG2a produced from Trichoplusia ni (TN-5B1-4, High Five) insect cells were characterized. Coexpression of the chaperone immunoglobulin heavy chain-binding protein (BiP) in the baculovirus-infected insect cells increased the soluble intracellular and secreted IgG level. This facilitated the detailed analysis of N-glycans from both intracellular and secreted IgG. Following purification of the immunoglobulins using Protein A-Sepharose, glycopeptides, prepared by trypsin-chymotrypsin digestion, were further digested with glycoamidase from sweet almond emulsin to obtain the oligosaccharide moieties. The resulting oligosaccharides were then reductively aminated with 2-aminopyridine and the structures identified by two-dimensional high performance liquid chromatography mapping (Tomiya, N., Awaya, J., Kurono, M., Endo, S., Arata, Y., and Takahashi, N. (1988) Anal. Biochem. 171, 73-90). The N-glycans obtained from the secreted IgG contain 35% complex type, some with terminal galactose residues at either alpha1, 3-Man or alpha1,6-Man branches of the Man3GlcNAc2 core. The remaining oligosaccharides detected in the secreted IgG were principally hybrid (30%) and paucimannosidic (35%) type N-glycans. Most (84%) of these secreted glycoforms contained fucose alpha1, 6-linked to the innermost GlcNAc residue and the presence of a potentially allergenic fucose alpha1,3-linked to the innermost GlcNAc residue was also detected. In contrast, the intracellular immunoglobulins included 50% high mannose-type N-glycans with lower levels of complex, hybrid, and paucimannosidic-type structures. Reverse phase one-dimensional high performance liquid chromatography analysis of the IgG N-glycans in the absence of heterologous BiP exhibited a similar distribution of intracellular and secreted glycoforms. These studies indicate that Trichoplusia ni TN-5B1-4 cells are capable of terminal galactosylation. However, the processing pathways in these cell lines appear to diverge from mammalian cells in the formation of paucimannosidic structures, in the presence of alpha1,3-fucose linkages, and in the absence of sialylation.
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PMID:Differential N-glycan patterns of secreted and intracellular IgG produced in Trichoplusia ni cells. 908 32

The removal of noncovalently bound polysaccharide coating from the extracellular enzymes of Aspergillus niger, by the technique of compartmental electrophoresis, had a very dramatic effect on the stability of beta-glucosidase. The polysaccharide-beta-glucosidase complex was extremely resistant to proteinases and far more stable against urea and temperature as compared with polysaccharide-free beta-glucosidase. The beta-glucosidase-polysaccharide complex was 18-, 36-, 40- and 82-fold more stable against chymotrypsin, 3 mol/L urea, total thermal denaturation and irreversible thermal denaturation, respectively, as compared with polysaccharide-free beta-glucosidase. The activation energy of polysaccharide-complexed beta-glucosidase (55 kJ/mol) was lower than polysaccharide-free enzyme (61 kJ/mol), indicating a slight activation of the enzyme by the polysaccharide. No significant difference could be detected in the specificity constant (V/K(m)) for A-nitrophenyl beta-D-glucopyranoside between polysaccharide-free and polysaccharide-complexed beta-glucosidase. We suggest that the function of these polysaccharides secreted by fungi including A. niger might be to protect the extracellular enzymes from proteolytic degradation, hence increasing their life span.
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PMID:The stability of extracellular beta-glucosidase from Aspergillus niger is significantly enhanced by non-covalently attached polysaccharides. 913 91


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