Coprecipitation of carbonic anhydrase by 1,1-bis(p-chlorophenyl)-2,2,2-trichloroethane, 1,1-bis(p-chlorophenyl)-2,2-dichloroethylene, and Dieldrin

Pocker, Y.; Beug, Michael W.; Ainardi, V. R.

doi:10.1021/bi00784a018

Cited by 23 publications

(2 citation statements)

References 30 publications

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“…On the other hand, the plant enzyme has a molecular weight of 180,000 and is made up of 6, possibly identical, subunits whose zinc analysis indicates the presence of 1 zinc atom/29,000 molecular weight subunit (CA from parsley leaves, Tobin, 1970; CA from spinach leaves, Y. Pocker and Mrs, J. Ng, unpublished results; cf. also Pocker et al, 1971). Although a powerful catalyst for the reversible hydration of carbon dioxide, the enzyme from spinach leaves does not show the catalytic versatility associated with the mammalian enzymes and is furthermore subject to regulatory control (Y. Pocker and Mrs. J.…”

Section: Discussionmentioning

confidence: 99%

Catalytic versatility of erythrocyte carbonic anhydrase. IX. Kinetic studies of the enzyme-catalyzed hydrolysis of 3-pyridyl and nitro-3-pyridyl acetates

Pocker¹,

Watamori²

1971

Biochemistry

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The present investigation demonstrates that bovine carbonic anhydrase powerfully catalyzes the hydrolysis of 3acetoxypyridine, 3-acetoxy-2-nitropyridine, and 3-acetoxy-2,6-dinitropyridine. The reactions follow Michaelis-Menten kinetics over the whole range of substrate concentrations studied, including the region [S] > Km. The pH-activity profiles are approximately sigmoid; the esterase activity is very small below pH 6 and rises to an intermediate plateau above pH 8. The inflection point at 25.0°lies at pH 7.56 for 3-acetoxy-2-nitropyridine and pH 7.4 for 3-acetoxy-2,6-dinitropyridine. A more detailed treatment of the data shows that for all these substrates the mild variation of Km with pH is dictated by the respective turnover number (ki) while the formal binding constants (ki/k-i) are nearly independent of pH

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Section: Discussionmentioning

confidence: 99%

Catalytic versatility of erythrocyte carbonic anhydrase. IX. Kinetic studies of the enzyme-catalyzed hydrolysis of 3-pyridyl and nitro-3-pyridyl acetates

Pocker¹,

Watamori²

1971

Biochemistry

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“…0.003% EDTA, pH 8.2 [28], An Orion Model 801A digital Ionalyzer fitted with a Sigma combination pH elec trode was used to determine the endpoint of pH 6.5 [29], Activity units (Wilbur-Anderson units) were cal culated according to Rickli et al [30].…”

Section: Enzyme Assaysmentioning

confidence: 99%

Role of Carbonic Anhydrase in Bone Resorption Induced by Prostaglandin E<sub>2</sub> vitro

Hall

Kenny

1985

Pharmacology

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The possible role of carbonic anhydrase in bone resorption induced by prostaglandin E₂ (PGE₂) was studied using an in vitro neonatal mouse calvarial culture system. PGE₂ (10^–6M) was effective in stimulating resorption, as assessed by calcium release into culture media. This enhanced resorption was accompanied by significant increases in calvarial carbonic anhydrase activity over control values at 48 and 96 h. At 48 h, bones treated with PGE₂ had 20% more carbonic anhydrase activity than controls. By 96 h, treated bones contained 79% more carbonic anhydrase activity than controls. PGE₂-induced bone resorption was inhibited by the carbonic anhydrase inhibitor acetazolamide in a dose-dependent fashion from 10^–5 to 10^–4M, with 77% inhibition observed at 10^–4M. The acetazolamide analogue CL 13,850 (N-t-butylacetazolamide), which does not inhibit carbonic anhydrase, failed to inhibit PGE₂-induced resorption. These results are consistent with the hypothesis that carbonic anhydrase is a necessary component of the osteoclastic bone resorptive mechanism.

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Carbonic Anhydrase: Structure, Catalytic Versatility, and Inhibition

Pocker

Sarkanen

1979

Advances in Enzymology - And Related Areas of Molecular Biology

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Coprecipitation of carbonic anhydrase by 1,1-bis(p-chlorophenyl)-2,2,2-trichloroethane, 1,1-bis(p-chlorophenyl)-2,2-dichloroethylene, and Dieldrin

Abstract: during the tenure of this work. Taken in part from the thesis of M. W. Beug to be submitted to the University of Washington in partial fulfillment of the Ph.D. degree.

Cited by 23 publications

References 30 publications

Catalytic versatility of erythrocyte carbonic anhydrase. IX. Kinetic studies of the enzyme-catalyzed hydrolysis of 3-pyridyl and nitro-3-pyridyl acetates

Catalytic versatility of erythrocyte carbonic anhydrase. IX. Kinetic studies of the enzyme-catalyzed hydrolysis of 3-pyridyl and nitro-3-pyridyl acetates

Role of Carbonic Anhydrase in Bone Resorption Induced by Prostaglandin E<sub>2</sub> vitro

Carbonic Anhydrase: Structure, Catalytic Versatility, and Inhibition

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