Inhibition of glycosidases by aldonolactones of corresponding configuration. The C-4- and C-6-specificity of <i>β</i>-glucosidase and <i>β</i>-galactosidase

Conchie, J.; Gelman, A. L.; Levvy, G. A.

doi:10.1042/bj1030609

Cited by 137 publications

(44 citation statements)

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“…The protein content shown is for cell walls isolated by the Kivilaan procedure (16). Cell walls isolated by the Kivilaan procedure but then water washed were similar having 7.9, 6.7, and 6.1% (w/w) protein, respectively, for the 0-to 5-mm, 6-to 10-mm and 11-to 15-mm sections. These results are also in agreement with those of King and Bayley (14) for walls prepared by the same method and with the same tissue but using Kjeldahl analysis.…”

Section: Resultsmentioning

confidence: 92%

“…However, if activities are expressed on a protein basis, the ratios of the specific activities for the various sections are not changed significantly. The specific activities of f3-glucosidase on a protein basis are 0.78, 0.22, and 0.23 nmoles of PNP liberated/pg of protein hr for water-washed glycerol-prepared walls and 10.9, 8, and 5 nmoles of PNP liberated/ag of protein -hr from the 0-to 5-mm, 6-to 10-mm, and 11 (39) 5-mm, 6-to 10-mm, and 11-to 15-mm sections, respectively, whereas the relative growth rates for the same regions were 100, 15, and 2, respectively. The relative distribution of ,B-glucosidase, a-galactosidase, acid phosphatase, and ,3-galactosidase activities in the various fractions from the aqueous cell wall preparations are shown in Table II.…”

Section: Resultsmentioning

confidence: 99%

“…These results are also in agreement with those of King and Bayley (14) for walls prepared by the same method and with the same tissue but using Kjeldahl analysis. Interestingly, walls prepared by an 900 / The values for aqueous walls refer to the activity observed for the aqueous homogenization and centrifugation procedure (the procedure commonly used in cell wall studies) gives protein contents of 14, 9, and 14% (w/w), respectively, for the 0-to 5-mm, 6-to 10-mm and 11-to 15-mm sections. This indicates the degree of contamination by membrane or cytoplasmic proteins experienced in the commonly used methods.…”

Section: Resultsmentioning

confidence: 99%

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Correlative Studies of Cell Wall Enzymes and Growth

Murray

Bandurski²

1975

Plant Physiol.

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If cell wall hydrolytic enzymes are involv-ed in extension growth, a correlation may be expected between hydrolytic activity of the cell walls and growth rate of the tissue from which the walls are prepared. Epicotyl sections from 0 to 5 mm, 6 to 10 mm, and 11 to 13 mm below the apical hook of pea seedlings (Pisum sativum var. Alaska) have relative growth rates of 100:15:2, respectivelv. The relative fl-glucosidase activities (units/mg wall) Data from several laboratories suggest that glycosidases play a role in wall plasticization, thus permitting cell elongation during extension growth (9). There is evidence that oligosaccharidehydrolyzing enzymes are localized in the walls (1,2,3,7,13,17,19,25) and that these enzymes can hydrolyze cell wall oligosaccharides (12,13, 15,18,25). It becomes important to know whether walllocalized glycosidase activity is correlated with the growth rate of the tissue from which the walls are prepared. Previous studies, mainly employing enzymes extracted from wall preparations (7,13,19,25), report that the amount of glycosidase activity correlates with the growth rate of the tissue from which the walls are prepared. In this current study, highly purified cell walls from Pisum epicotyls were utilized, thus permitting specific activity determinations. We find that (3-glucosidase specific activity is highest in walls from rapidly elongating tissue but that surface sterilized in 1 % sodium hypochlorite for 15 min, soaked in running tap water for 18 hr, and germinated on absorbent paper in covered plastic trays. Germination was in the dark at 25 C and 85c% relative humidity, and seedlings were harvested 84 hr after germination was begun. Growth rates of the seedlings were determined by marking at 2.5-mm intervals and subsequently measuring the spacings. Sequential epicotyl sections were taken from 0 to 5 mm, 6 to 10 mm, and 11 to 15 mm below the apical hook. The sections were either dropped into beakers on Dry Ice immediately after cutting in the case of samples for cell wall preparation by the nonaqueous method, or, in all other cases, they were weighed out in 0.5-g lots and then frozen on Dry Ice as soon as 0.5 g was obtained. The tissue was stored at -80 C until used.Cell Wall Preparation. Cell walls were prepared by homogenization in glycerol and filtration through a glass bead filter, as described by Kivilaan et al. (16). The wall material was dried in an evacuated dessicator over P205, CaCl2, and paraffin at 4 C for 24 to 48 hr. The resultant white powder was stored at -10 C in a sealed jar over CaSO4. Alternatively glycerol was removed from the pelleted walls by water, rather than by solvent washing, as in the Kivilaan procedure. Washing and collection by centrifugation was repeated three times, the cell wall material was collected by filtration, dried over P205 in vacuo, and stored as described above.Aqueous Cell Wall Preparation. Cell walls were also prepared by homogenization of 0.5-g aliquots of frozen tissue sections ground at 0 to 4 C in a 50-ml conical glass hom...

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Section: Resultsmentioning

confidence: 92%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Correlative Studies of Cell Wall Enzymes and Growth

Murray

Bandurski²

1975

Plant Physiol.

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“…30) The activities of Lysosomal enzymes cathepsin-D, 31) Acid phosphatase, 32) β-Dglucuronidase, 33) β-D-galactosidase 34) and β-Nacetyl glucosaminidase 35) were also studied. Electron Microscopic Studies --Small pieces of heart were taken and rinsed in 0.1 M phosphate buffer, pH 7.2.…”

Section: Plant Materials and Chemicals --Roots Ofmentioning

confidence: 99%

Protective Efficacy of Nardostachys jatamansi (Rhizomes) on Mitochondrial Respiration and Lysosomal Hydrolases during Doxorubicin Induced Myocardial Injury in Rats

Subashini

Arunachalam

Senthilkumar

et al. 2007

JOURNAL OF HEALTH SCIENCE

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Doxorubicin is highly effective in treatment for several forms of cancer. However, doxorubicin induces a cumulative and dose dependent cardiomyopathy that has been ascribed to redox-cycling of the molecule on the mitochondrial complex 1 generating in the process of increased oxidative stress. In the search of new potential cardioprotective agents, the present study is directed to explore the effect of ethanolic extract of Nardostachys jatamansi on the mitochondrial and lysosomal damage induced by doxorubicin in rats. Heart mitochondria were isolated from rats treated with doxorubicin (15 mg/kg, ip) a single dose, exhibited depressed rates of state 3 respiration, low respiratory control ratio (RCR), decreased Oxidative Phosphorylation ratio, Adenosine Triphosphate content and cytochromes (c, c 1 , b, aa 3 ). In addition the doxorubicin given rats showed significant changes in the lysosomal enzymes (Cathepsin-D, Acid phosphatase, β-D-glucoronidase, β-D-galactosidase and β-N-acetyl glucosaminidase) and membrane bound phosphatases. Also myocardial damage, as assessed by ultrastructural changes showed loss of myofibrils, mitochondrial swelling, and cytoplasmic vacuolization. Pretreatment with Nardostachys jatamansi (500 mg/kg body weight orally) for seven days ameliorated the observed abnormalities and significantly prevented the mitochondrial respiration, lysosomal integrity, membrane bound phosphatases and ultrastructural studies in doxorubicin induced rats. These findings suggest that the cardioprotective efficacy of Nardostachys jatamansi could be mediated possibly through its antioxidant effect as well as by the attenuation of the oxidative stress.

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“…Assay of β-glucosidase β-Glucosidase was assayed according to the method of Conchie et al (1967) based on the principle that β-glucosidase acts on p-nitrophenyl-β-D-glucopyranoside and liberates p-nitrophenol, which was measured at 410 nm in alkaline pH. The enzyme solution (0.2 mL) was added to 0.5 mL of substrate and 0.3 mL of citrate buffer in a test tube, shaken gently, and incubated at 37°C for 1 h. Glycine-NaOH buffer (3 mL) was added for reaction termination, mixed, and read at 410 nm using the Shimadzu UV-1601 spectrophotometer.…”

Section: Biochemical Assaysmentioning

confidence: 99%

Protective effect of betaine on changes in the levels of lysosomal enzyme activities in heart tissue in isoprenaline-induced myocardial infarction in Wistar rats

Ganesan

Anandan

2009

Cell Stress and Chaperones

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Myocardial infarction is one of the most common manifestations of cardiovascular disease. In the present study, we investigated the protective effect of betaine, a potent lipotropic molecule, on changes in the levels of lysosomal enzymes and lipid peroxidation in isoprenalineinduced myocardial infarction in Wistar rats, an animal model of myocardial infarction in man. Male albino Wistar rats were pretreated with betaine (250 mg/kg body weight) daily for a period of 30 days. After the treatment period, isoprenaline (11 mg/100 g body weight) was intraperitoneally administered to rats at intervals of 24 h for 2 days. The activities of lysosomal enzymes (β-glucuronidase, β-galactosidase, β-glucosidase, and acid phosphatase) were significantly (p<0.05) increased in plasma with a concomitant decline in the activities of these enzymes in heart tissue of isoprenaline-administered rats. Also, the level of lipid peroxidation was higher in heart lysosomes of isoprenaline-injected rats. Pretreatment with betaine daily for a period of 30 days to isoprenaline-induced rats prevented the changes in the activities of these lysosomal enzymes. Oral treatment with betaine (250 mg/kg body weight) to normal control rats did not show any significant effect in all the biochemical parameters studied. Thus, the results of our study show that betaine protects the lysosomal membrane against isoprenaline-induced myocardial infarction. The observed effects might be due to the free radical-scavenging and membrane-stabilizing properties of betaine.

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Inhibition of glycosidases by aldonolactones of corresponding configuration. The C-4- and C-6-specificity of β-glucosidase and β-galactosidase

Cited by 137 publications

References 9 publications

Correlative Studies of Cell Wall Enzymes and Growth

Correlative Studies of Cell Wall Enzymes and Growth

Protective Efficacy of Nardostachys jatamansi (Rhizomes) on Mitochondrial Respiration and Lysosomal Hydrolases during Doxorubicin Induced Myocardial Injury in Rats

Protective effect of betaine on changes in the levels of lysosomal enzyme activities in heart tissue in isoprenaline-induced myocardial infarction in Wistar rats

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