Amino acid composition of various forms of bovine and human erythrocyte carbonic anhydrase

Nyman, Per-Olof; Lindskog, Sven

doi:10.1016/0926-6569(64)90174-9

Cited by 109 publications

(67 citation statements)

References 27 publications

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“…CA I and CA I1 are major isoforms in red blood cells, and they are known as the low-activity isoenzyme and the high-activity isozyme, respectively (13). CA 111 is a muscle type of CA (14,15), while CA IV is a so-called membrane-bound form of CA and is distributed in (19).…”

Section: Discussionmentioning

confidence: 99%

Antibodies to Carbonic Anhydrase in Systemic Lupus Erythematosus and Other Rheumatic Diseases

Itoh

Reichlin

1992

Arthritis & Rheumatism

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Objective. Autoantibodies to CA were demonstrated in the sera of patients with systemic lupus erythematosus (SLE) and some other rheumatic diseases. This study was undertaken to define the isoform and species specificity of these reactions, as well as to develop a method for detecting immune complexes. Methods. Antibodies to CA were sought by enzyme‐linked immunosorbent assay (ELISA) and by Western immunoblotting. Results. An increased prevalence of CA autoantibodies was detected, by both methods, in patients with SLE, scleroderma, and polymyositis, compared with controls. In SLE patients, CA autoantibodies occurred preferentially in those with anti—U1 RNP or anti‐U1 RNP and Ro/SS‐A. Some sera reacted with only the CA 1 or CA II isoform, while ˜50% of sera that were CA positive reacted with both isoforms. The autoantibodies reacted preferentially with the human enzymes, rather than the bovine CA, both on Western blot and by ELISA. Selected IgG F(ab')2 fragments from anti‐CA—containing sera specifically inhibited the enzyme activity of CA, and the CA inhibitor acetazolamide partially inhibited the binding of anti‐CA to CA. Thus, at least a part of autoanti‐CA is directed toward the active site of CA. Finally, CA molecules were detected as immune complexes in sera from selected anti‐CA‐positive patients. Conclusion. Autoantibodies to CA represent a previously unrecognized autoantibody to an abundant intracellular protein of the human erythrocyte.

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Section: Discussionmentioning

confidence: 99%

Antibodies to Carbonic Anhydrase in Systemic Lupus Erythematosus and Other Rheumatic Diseases

Itoh

Reichlin

1992

Arthritis & Rheumatism

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“…Enzyme concentrations were estimated spectrophotometrically at 280 nm taking al% = 18.7 cm -1 [5] and a • " 280 mol. wt.…”

Section: Ke2mentioning

confidence: 99%

The catalytic mechanism of human carbonic anhydrase C: Inhibition of CO₂ hydration and ester hydrolysis by HCO⁻₃

Steiner¹,

Jonsson²,

Lindskog³

1976

FEBS Letters

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“…Procedures spectrophotometrically at 280 mp taking the molecular extinction coefficient e2*/, = 57,000 M-l x cm-l and a molecular weight of 30,000 [17].…”

Section: Enzymementioning

confidence: 99%

Studies of the Esterase Activity and the Anion Inhibition of Bovine Zinc and Cobalt Carbonic Anhydrases

Thorslund¹,

Lindskog²

1967

European Journal of Biochemistry

158

109

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I. The rates of hydrolysis of nitrophenyl esters, catalyzed by bovine carbonic anhydrase, depend on the position of the nitro group and on the size of the acyl residue. The most rapidly hydrolyzed substrate of those investigated is p-nitrophenyl acetate. The catalyzed rates are proportional to both enzyme and ester concentrations. Only in the case of m-nitrophenyl acetate could a value of the Michaelis constant, K , , be estimated, approximately 10 mM. Product inhibition by o-nitrophenol occurs during the enzyme-catalyzed hydrolysis of o-nitrophenyl acetate.2 . The metal specificity of the enzyme seems to be independent of the substrate. Zn(I1) and Co(I1) are about equally effective in restoring esterase activity to the apoenzyme while all other metal ions studied do not activate or have a very small effect.3. The pH-dependence of the esterase activity of both Zn(I1)-and Co(I1)-carbonic anhydrase is very similar to that of the CO, hydration activity, and the basic form of a group with a pK near 7 is required for both reactions. Anionic inhibitors are strongly bound to the enzyme when this group is in its acidic form, but the inhibition is almost abolished a t alkaline pH.4. The inhibitory powers of cyanide and sulfide decrease a t acid as well as at alkaline pH. The results agree with the assumption that, formally, CN-and HS-do not bind to the basic form of the enzyme, while HCN and H,S do not bind to the acidic form.Carbonic anhydrase catalyses the reversible hydration of carbon dioxide with an exceptionally high turnover [l]. I n addition, the enzyme has been shown to act on a number of other carbonyl systems. Pocker and Meany reported the carbonic anhydrasecatalyzed hydration of acetaldehyde [2] and pyridine aldehydes [3,4]. The hydrolysis of certain esters is also catalyzed by the enzyme and this activity has been utilized by several investigators, who used p-nitrophenyl acetate (p-NPA) and other phenolic esters as substrates [5-lo]. Recently, a cyclic sulfonate ester has been shown to be an extraordinarily good substrate [ll] although still surpassed by carbon dioxide by several orders of magnitude.We have studied the kinetics of the hydrolysis of p-NPA and some related substrates to obtain further information about the catalytic mechanism of carbonic anhydrase. The apparent Michaelis constants for these substances are large and could not be determined due to the limited solubility of the substrates in water. Although it may not be feasible to use these Enzyme. Carbonic anhydrase or carbonate hydro-lyase (EC 4.2.1.1).

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Amino acid composition of various forms of bovine and human erythrocyte carbonic anhydrase

Cited by 109 publications

References 27 publications

Antibodies to Carbonic Anhydrase in Systemic Lupus Erythematosus and Other Rheumatic Diseases

Antibodies to Carbonic Anhydrase in Systemic Lupus Erythematosus and Other Rheumatic Diseases

The catalytic mechanism of human carbonic anhydrase C: Inhibition of CO₂ hydration and ester hydrolysis by HCO⁻₃

Studies of the Esterase Activity and the Anion Inhibition of Bovine Zinc and Cobalt Carbonic Anhydrases

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Amino acid composition of various forms of bovine and human erythrocyte carbonic anhydrase

Cited by 109 publications

References 27 publications

Antibodies to Carbonic Anhydrase in Systemic Lupus Erythematosus and Other Rheumatic Diseases

Antibodies to Carbonic Anhydrase in Systemic Lupus Erythematosus and Other Rheumatic Diseases

The catalytic mechanism of human carbonic anhydrase C: Inhibition of CO2 hydration and ester hydrolysis by HCO−3

Studies of the Esterase Activity and the Anion Inhibition of Bovine Zinc and Cobalt Carbonic Anhydrases

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The catalytic mechanism of human carbonic anhydrase C: Inhibition of CO₂ hydration and ester hydrolysis by HCO⁻₃