Purification and properties of an acid phosphatase from bovine brain

Chaimovich, Hernán; Nome, Faruk

doi:10.1016/0003-9861(70)90039-1

Cited by 41 publications

(11 citation statements)

References 20 publications

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“…The lysosomal AcP was sensitive to EDT A, the micro somal AcP to NEM, and the cytosol AcP fraction to both EDTA and NEM. The inability of NEM to inhibit lysosomal AcP (Chaimovich and Nome, 1970) and the EDT A stimulation of lysosomal AcP (Lieberherr et aI., 1973) and other observations ap pear consistent with the literature. These results, together with the appearance of the cytosolic en zyme PST only in the cytosol fraction (Baranczyk Kuzma et aI.…”

Section: Discussionsupporting

confidence: 85%

Demonstration of Acid Hydrolase Activity in Primary Cultures of Bovine Brain Microvessel Endothelium

Barańczyk‐Kuźma

Raub

Audus

1989

J Cereb Blood Flow Metab

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The existence of lysosomes and acid hydrolase activity was demonstrated in an in vitro blood-brain barrier (BBB) model comprising primary cultures of bovine brain microvessel endothelial cell (BMEC) monolayers. BMEC lysosomes were observed by the uptake of acridine orange and fluorophore-labeled acetylated low-density lipoprotein by fluorescence microscopy. Cytochemical localization of the acid hydrolase, sulfatase, and acid phosphatase (AcP) activities with light microscopy also revealed hydrolase-positive vacuoles or lysosomes that varied in number from cell to cell. BMEC monolayers were fractionated and biochemical assays of the sulfatase, AcP, and beta-galactosidase were performed. Significant activities of the acid hydrolases were found to be associated with lysosome and microsome fractions (69-77%). The majority of beta-galactosidase (approximately 48%) and total sulfatase (approximately 58%) activity was associated with the lysosome fraction of the BMECs. In contrast, approximately 52% of AcP activity was associated with the microsome fraction of the cells. The results of this study are consistent with the demonstration in vivo of acid hydrolases as potential factors in the endocytic pathway for transport of proteins through the BBB and as contributors to the BBB's enzymatic barrier function.

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Section: Discussionsupporting

confidence: 85%

Demonstration of Acid Hydrolase Activity in Primary Cultures of Bovine Brain Microvessel Endothelium

Barańczyk‐Kuźma

Raub

Audus

1989

J Cereb Blood Flow Metab

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“…The pNP released was measured at 405 nm in a UNICAM 8625 UV/VIS spectrophotometer. For the initial velocity (V) determination, the amount of pNP produced was calculated using a molar extintion coefficient of 18,300 M -1 cm -1 (Chaimovich and Nome 1970). Units (U) of enzymatic activity are defined as lmoles of pNP released per min.…”

Section: Assay Of Phosphatase Activitymentioning

confidence: 99%

Effect of copper on the activation of the acid phosphatase from the green algae Pseudokirchneriella subcapitata

Jonsson

Aoyama

2009

Biometals

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The presence of copper in water environment may have detrimental effects on aquatic organisms, including algae, where different enzymatic systems can be affected. Algae acid phosphatase plays important roles in metabolic processes such as decomposition of organic phosphate, autophagic digestive process, recycling cellular materials and zygote formation during reproduction. This work describes an in vitro activation effect of copper on the acid phosphatase of the green algae Pseudokirchneriella subcapitata (formely Selenastrum capricornutum) under preincubation condition. Apparent Michaelis constant values of 1.21 and 0.37 mM, and activation energy values of 26.8 and 13.6 kJ mol(-1) were determined in the absence and in the presence of 0.2 mM Cu(2+), respectively. The dissociation constant value for Cu(2+) binding to the enzyme was determined to be 22.04 microM. The decrease of the apparent Michaelis constant (Km) and activation energy values in the presence of Cu(2+) correlates well with its activating effect on the acid phosphatase activity. This propriety could be used as a sensitive bioindicator for copper in environmental samples.

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“…The pNP released was measured at 405 nm in a UNICAM 8625 UV/VIS spectrophotometer. For the initial velocity [V] determination, the amount of pNP produced was calculated using a molar extinction coefficient of 18,300 M -1 cm -1 (Chaimovich and Nome 1970). Units (U) of enzymatic activity are defined as micromoles of pNP released per min.…”

Section: Assay Of Phosphatase Activitymentioning

confidence: 99%

Metals and linear alkylbenzene sulphonate as inhibitors of the algae Pseudokirchneriella subcapitata acid phosphatase activity

Jonsson¹,

Paraíba²,

Aoyama³

2009

Ecotoxicology

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Sewage sludge applied to soils as a fertilizer often contains metals and linear alkylbenzene sulphonate (LAS) as contaminants. These pollutants can be transported to the aquatic environment where they can alter the phosphatase activity in living organisms. The acid phosphatase of algae plays important roles in metabolism such as decomposing organic phosphate into free phosphate and autophagic digestive processes. The order of in vitro inhibition of Pseudokirchneriella subcapitata acid phosphatase at the highest concentration tested was LAS > Hg2+ = Al3+ > Se4+ = Pb2+ > Cd2+. A non-competitive inhibition mechanism was obtained for Hg2+ (Ki = 0.040 mM) and a competitive inhibition for LAS (Ki = 0.007 mM). In vivo studies with treated algae cultures showed that the inhibition of specific activity was observed in algae exposed during 7 days, in contrast to short term (24 h) treatments with both these chemicals. Our results suggest that the inhibition parameters in vitro did not markedly differ between the two chemicals. On the other hand, in vivo evaluations showed strong differences between both pollutants regarding the concentration values and the degree of response.

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Purification and properties of an acid phosphatase from bovine brain

Cited by 41 publications

References 20 publications

Demonstration of Acid Hydrolase Activity in Primary Cultures of Bovine Brain Microvessel Endothelium

Demonstration of Acid Hydrolase Activity in Primary Cultures of Bovine Brain Microvessel Endothelium

Effect of copper on the activation of the acid phosphatase from the green algae Pseudokirchneriella subcapitata

Metals and linear alkylbenzene sulphonate as inhibitors of the algae Pseudokirchneriella subcapitata acid phosphatase activity

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