scholarly journals Hydrolysis of a naturally occurring β-glucoside by a broad-specificity β-glucosidase from liver

1986 ◽  
Vol 237 (2) ◽  
pp. 469-476 ◽  
Author(s):  
K L LaMarco ◽  
R H Glew
Keyword(s):  
Guinea Pig ◽  
Competitive Inhibitor ◽  
Heat Denaturation ◽  
Pig Liver ◽  
Naturally Occurring ◽  
Aryl Glycosides ◽  
Beta Glucosidase ◽  
Hydrolysis Of ◽  
Guinea Pig Liver ◽  
Broad Specificity

We have isolated from guinea-pig liver a broad-specificity beta-glucosidase of unknown function that utilizes as its substrate non-physiological aryl glycosides (e.g. 4-methylumbelliferyl beta-D-glucopyranoside, p-nitrophenyl beta-D-glucopyranoside). The present paper documents that this enzyme can be inhibited by various naturally occurring glycosides, including L-picein, dhurrin and glucocheirolin. In addition, L-picein, which acts as a competitive inhibitor of the broad-specificity beta-glucosidase (Ki 0.65 mM), is also a substrate for this enzyme (Km 0.63 mM; Vmax. 277,000 units/mg). Heat-denaturation, kinetic competition studies, chromatographic properties and pH optima all argue strongly that the broad-specificity beta-glucosidase is responsible for the hydrolysis of both the non-physiological aryl glycosides and L-picein. This paper demonstrates that beta-glucosidase can catalyse the hydrolysis of a natural glycoside, and may provide a key to understanding the function of this enigmatic enzyme. A possible role in the metabolism of xenobiotic compounds is discussed.

scholarly journals Exolytic hydrolysis of toxic plant glucosides by guinea pig liver cytosolic beta-glucosidase.

1992 ◽  
Vol 267 (20) ◽  
pp. 14027-14032
Author(s):  
V Gopalan ◽  
A Pastuszyn ◽  
W R Galey ◽  
R.H. Glew
Keyword(s):  
Guinea Pig ◽  
Pig Liver ◽  
Beta Glucosidase ◽  
Toxic Plant ◽  
Hydrolysis Of ◽  
Guinea Pig Liver

scholarly journals THE OCCURRENCE AND DISTRIBUTION OF ATROPINESTERASE, AND THE SPECIFICITY OF TROPINESTERASES

1941 ◽  
Vol 25 (2) ◽  
pp. 197-205 ◽  
Author(s):  
David Glick ◽  
Susi Glaubach
Keyword(s):  
Guinea Pig ◽  
Egg White ◽  
Pig Liver ◽  
Naturally Occurring ◽  
Hydrolysis Of ◽  
Guinea Pig Liver

Atropinesterase was found to exist in approximately one out of every four rabbits, and no relation could be observed between the incidence of the enzyme and season, sex, color, age, or weight. The occurrence of the enzyme was also shown to be unrelated to that of cholinesterase. The distribution of atropinesterase in the blood and organs of rabbits was studied; the animals devoid of the enzyme in their blood contained no demonstrable activity in any of the organ extracts tested. The presence of atropinesterase in frog liver, and its absence from the serum, has been confirmed. Hydrolysis of homatropine, but not atropine, by guinea pig liver was observed, while the serum was without action on either of the compounds. On this basis the possibility arises that guinea pig liver contains a homatropinesterase enzyme separate from atropinesterase. It was shown that lack of atropinesterase activity in certain rabbits is not likely to be due to the presence of a naturally occurring inhibitor. It has been demonstrated that contrary to previous indications neither fresh egg white nor yolk possess atropinesterase activity. The specificity of tropinesterases was investigated and evidence was presented for the possible existence of two distinct enzymes, cocainesterase and tropacocainesterase.

scholarly journals Human glucocerebrosidase catalyses transglucosylation between glucocerebroside and retinol

1994 ◽  
Vol 300 (2) ◽  
pp. 309-315 ◽  
Author(s):  
D J Vanderjagt ◽  
D E Fry ◽  
R H Glew
Keyword(s):  
Guinea Pig ◽  
Incubation Medium ◽  
Alternative Pathway ◽  
Pig Liver ◽  
Hydrolytic Reaction ◽  
Endogenous Lipid ◽  
Sodium Taurodeoxycholate ◽  
Beta Glucosidase ◽  
Guinea Pig Liver ◽  
Broad Specificity

The basal activity of human placental glucocerebrosidase is elevated 16-fold by n-pentanol when assayed using p-nitrophenyl beta-D-glucopyranoside (pNPGlc) as the beta-glucosidase substrate. This enhancement of activity is the result of the formation of a transglucosylation product, n-pentyl beta-D-glucoside, in rate-determining competition with the hydrolytic reaction. The transglucosylation product accounts for approximately 80% of the reaction product generated in the presence of n-pentanol (0.18 M) when either glucocerebroside or pNPGlc was used as the substrate. This stimulatory effect can be increased an additional 3-fold by the inclusion of phosphatidylserine (20 micrograms/ml) or sodium taurodeoxycholate (0.3%, w/v) in the incubation medium. In the presence of retinol, glucocerebrosidase also catalyses the synthesis of a novel lipid glucoside, retinyl glucoside, when either glucocerebroside or pNPGlc serves as the substrate. The reaction product was identified as retinyl beta-D-glucoside, based on its susceptibility to hydrolysis by almond beta-D-glucosidase and the subsequent release of equimolar amounts of retinol and glucose. The rate of retinyl-beta-glucoside formation is dependent on the concentration of retinol in the incubation medium, reaching saturation at approximately 0.3 mM retinol. Retinyl beta-D-glucoside is a substrate for two broad-specificity mammalian beta-glucosidases, namely the cytosolic and membrane-associated beta-glucosidases of guinea pig liver. However, retinyl beta-D-glucoside is not hydrolysed by placental glucocerebrosidase. These data indicate that the glucocerebrosidase-catalysed transfer of glucose from glucocerebroside to natural endogenous lipid alcohols, followed by the action of a broad-specificity beta-glucosidase on the transglucosylation product, could provide mammals with an alternative pathway for the breakdown of glucocerebroside to glucose and ceramide.

scholarly journals Photoaffinity labelling of nucleoside-transport proteins in plasma membranes isolated from rat and guinea-pig liver

1984 ◽  
Vol 220 (2) ◽  
pp. 499-506 ◽  
Author(s):  
J S R Wu ◽  
J D Young
Keyword(s):  
Guinea Pig ◽  
Plasma Membranes ◽  
Species Difference ◽  
Sodium Dodecyl ◽  
Competitive Inhibitor ◽  
Nucleoside Transport ◽  
Nucleoside Transporter ◽  
Pig Liver ◽  
Liver Homogenates ◽  
Guinea Pig Liver

Nitrobenzylthioinosine (NBMPR) was employed as a probe of the nucleoside transporters from rat and guinea-pig liver. Purified liver plasma membranes prepared on self-generating Percoll density gradients exhibited 16-fold (rat) and 10-fold (guinea pig) higher [3H]NBMPR-binding activities than in crude liver homogenates (3.69 and 14.7 pmol/mg of protein for rat and guinea-pig liver membranes respectively, and 0.23 and 1.47 pmol/mg of protein for crude liver homogenates respectively). Binding to membranes from both species was saturable (apparent Kd 0.14 and 0.63 nM for rat and guinea-pig membranes respectively) and inhibited by uridine, adenosine, nitrobenzylthioguanosine (NBTGR) and dilazep. Uridine was an apparent competitive inhibitor of high-affinity NBMPR binding to rat membranes (apparent Ki 1.5 mM). There was a marked species difference with respect to dipyridamole inhibition of NBMPR binding (50% inhibition at 0.2 and greater than 100 microM for guinea-pig and rat respectively). These results are consistent with a role of NBMPR-binding proteins in liver nucleoside transport. Exposure of rat and guinea pig membranes to high-intensity u.v. light in the presence of [3H]NBMPR resulted in the selective radio-labelling of membrane proteins which migrated on sodium dodecyl sulphate/polyacrylamide gels with apparent Mr values in the same range as that of the human erythrocyte nucleoside transporter (45 000-66 000). Covalent labelling of these proteins was abolished when photolysis was performed in the presence of non-radio-active NBTGR as competing ligand.

Die Bedeutung der Homogenisationsart und -intensität für die Größe und Konstanz der Sauerstoffaufnahme von Meerschweinchen-Leberhomogenat / The Influence of Mode and Intensity of Homogenization on the Absolute Value and Stability of Oxygen Consumption of Guinea Pig Liver Homogenates

1977 ◽  
Vol 32 (11-12) ◽  
pp. 908-912 ◽  
Author(s):  
H. J. Schmidt ◽  
U. Schaum ◽  
J. P. Pichotka
Keyword(s):  
Oxygen Uptake ◽  
Guinea Pig ◽  
Measuring Time ◽  
Pig Liver ◽  
Absolute Value ◽  
Modified Method ◽  
Simultaneous Measurements ◽  
Liver Homogenates ◽  
The Absolute ◽  
Guinea Pig Liver

Abstract The influence of five different methods of homogenisation (1. The method according to Potter and Elvehjem, 2. A modification of this method called Potter S, 3. The method of Dounce, 4. Homogenisation by hypersonic waves and 5. Coarce-grained homogenisation with the “Mikro-fleischwolf”) on the absolute value and stability of oxygen uptake of guinea pig liver homogenates has been investigated in simultaneous measurements. All homogenates showed a characteristic fall of oxygen uptake during measuring time (3 hours). The modified method according to Potter and Elvehjem called Potter S showed reproducible results without any influence by homogenisation intensity.

Precision-cut Guinea-pig Liver Slices as a Tool for Studying the Toxicity of Volatile Anaesthetics

1990 ◽  
Vol 18 (1_part_1) ◽  
pp. 191-199
Author(s):  
Hanan N. Ghantous ◽  
Jeanne Fernando ◽  
Scott E. Morgan ◽  
A. Jay Gandolfi ◽  
Klaus Brandel
Keyword(s):  
Guinea Pig ◽  
Rank Order ◽  
Normal Liver ◽  
Liver Slice ◽  
Volatile Anaesthetics ◽  
Pig Liver ◽  
Liver Slices ◽  
Guinea Pig Liver ◽  
Krebs Henseleit Buffer

Cultured precision-cut liver slices retain normal liver architecture and physiological biochemical functions. Hartley male guinea-pig liver slices have proven to be a good model for studying the biotransformation and toxicity of halothane. This system was used to evaluate the biotransformation and toxicity of different volatile anaesthetics (halothane, enflurane, isoflurane and sevoflurane), and compare their effects to those of new anaesthetics (desflurane). Liver slices (250–300μm thick) were incubated in sealed roller vials, containing Krebs Henseleit buffer at 37°C under 95% O2:5% CO2 atmosphere. Volatile anaesthetics were delivered by volatilisation after pre-incubation for 1 hour to produce a constant concentration in the medium. Production of the metabolites, trifluroacetic acid and fluoride ion, was measured. Intracellular potassium ion content, protein synthesis and secretion were determined as indicators of viability of the slices. The rank order of biotransformation of anaesthetics by the liver slices was halothane >sevoflurane>isoflurane and enflurane>desflurane. The rank order of hepatotoxicity of these anaesthetics was halothane>isoflurane and enflurane>sevoflurane and desflurane. Halothane is the anaesthetic which is metabolised furthest and has the most toxic effect, while desflurane is the least metabolised anaesthetic and has the least toxicity. This in vitro cultured precision-cut liver slice system appears to be suitable for studying the biotransformation of volatile anaesthetics and correlating its role in the resulting toxicity.

scholarly journals THE REDUCTION OF l-XYLULOSE TO XYLITOL BY GUINEA PIG LIVER MITOCHONDRIA

1956 ◽  
Vol 221 (2) ◽  
pp. 697-709 ◽  
Author(s):  
Oscar Touster ◽  
V.H. Reynolds ◽  
Ruth M. Hutcheson
Keyword(s):  
Guinea Pig ◽  
Liver Mitochondria ◽  
Pig Liver ◽  
Guinea Pig Liver
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