Kinetics and inhibition of membrane-bound carbonic anhydrase from canine renal cortex

Sanyal, Gautam; Pessah, Ness I.; Maren, Thomas H.

doi:10.1016/0005-2744(81)90136-4

Cited by 57 publications

(24 citation statements)

References 10 publications

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“…The N-terminal sequence ofthe purified protein is preceded by an additional 34 aa in the deduced sequence. This 34-aa peptide contains properties that are characteristic of signal sequences in secretory proteins from the Bacteria and Eucarya domains (31); the central hydrophobic region (positions [7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26] in Fig. 3) is flanked by two hydrophilic regions with the N-terminal one containing a positively charged amino acid (position 5 in Fig.…”

Section: Resultsmentioning

confidence: 99%

A carbonic anhydrase from the archaeon Methanosarcina thermophila.

Alber

Ferry

1994

Proc. Natl. Acad. Sci. U.S.A.

237

188

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Carbonic anhydrase (CA) from acetategrown Methanosawina thermophila was purified >10,000-fold (22% recovery) to apparent homogeneity with a specific activity of 4872 units/mg. The estimated native molecular mass of the enzyme is 84 kDa based on gel filtration chromatography. SDS/PAGE revealed one protein band with an apparent molecular mass of 40 kDa. The M. thermophila CA is less sensitive than human CA isozyme H toward inhibition by sulfonamides and monovalent Ions. The gene encing this CA was cloned into pUC18 and sequenced. Escherichia coH harboring the recombinant plasmid expresses CA activity (2.3 units/mg of cell extract protein). Comparison of the deduced amino acid sequence with the N-terminal sequence of the purified protein shows that the gene encodes an additional 34 N-terminal residues with properties characteristic of signal peptides in secretory proteins. The calculated molular mass (22.9 kDa) and pl (4.0) suggest that SDS/PAGE overestimates the subunit size and that the native enzyme is a tetramer. To our knowledge, the deduced amino acid sequence has no signicant identity to any known CA but has 35% sequence identity to the first 197 deduced N-terminal amino acids of a proposed C02-concentrating-anism protein from Synechococcus PCC7942 and 28% sequence identity to the deduced sequence of ferripyochelin binding protein from Pseudomonas aeruginosa. Thus, our results indicate that this archaeal CA represents a distinct class of CAs and provide a basis to determine physiological roles for CA in acetotrophic anaerobes.

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Section: Resultsmentioning

confidence: 99%

A carbonic anhydrase from the archaeon Methanosarcina thermophila.

Alber

Ferry

1994

Proc. Natl. Acad. Sci. U.S.A.

237

188

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“…A proximal component was suggested by HC03-wasting at normal plasma concentrations (i.e. a low Tm for HC03-) (12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25). A distal defect, profound in some patients, was evident from their inadequate ability to acidify their urine, even while quite acidotic…”

Section: Discussionmentioning

confidence: 99%

“…The renal response to infused acetazolamide in these patients is of great interest since CA I1 is the only soluble CA isozyme identified in the kidney (7)(8)(9), and its absence apparently is responsible for the mixed or hybrid-type RTA in CA IIdeficient patients (10)(11)(12)(13)(14)(15). However, there have been recent reports of a less well-characterized, membrane-bound luminal CA in the brush border of the proximal tubule of the kidney (1 6,17). The luminal CA appears to play an important role in the reclamation of filtered HC03-and is known to be sensitive to inhibition by acetazolamide (1 8, 19).…”

mentioning

confidence: 99%

Positive Renal Response to Intravenous Acetazolamide in Patients with Carbonic Anhydrase II Deficiency

et al. 1985

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“…Sera were also obtained from 24 patients with primary Sjogren's syndrome (SS), 28 with rheumatoid arthritis (RA), 28 with PM, and 28 with SSc. Sera were stored for later use at -20°C.…”

Section: Methodsmentioning

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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Kinetics and inhibition of membrane-bound carbonic anhydrase from canine renal cortex

Cited by 57 publications

References 10 publications

A carbonic anhydrase from the archaeon Methanosarcina thermophila.

A carbonic anhydrase from the archaeon Methanosarcina thermophila.

Positive Renal Response to Intravenous Acetazolamide in Patients with Carbonic Anhydrase II Deficiency

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

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