Effect of physical exercise on the specific activity of carbonic anhydrase isozyme in human erythrocytes

1982 ◽  
Vol 38 (7) ◽  
pp. 830-831 ◽  
Author(s):  
H. Ohno ◽  
N. Taniguchi ◽  
T. Kondo ◽  
E. Takakuwa ◽  
K. Terayama ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Physical Exercise ◽  
Specific Activity ◽  
Human Erythrocytes ◽  
Carbonic Anhydrase Isozyme

Zinc Deficiency States and Carbonic Anhydrase Isozyme in Experimental Hemolytic and Bleeding Anemia of Rabbits

Enzyme ◽  
1981 ◽  
Vol 26 (2) ◽  
pp. 85-92 ◽  
Author(s):  
Naoki Ishikawa ◽  
Tadao Shiraishi ◽  
Takahito Kondo ◽  
Naoyuki Taniguchi
Keyword(s):  
Carbonic Anhydrase ◽  
Zinc Deficiency ◽  
Carbonic Anhydrase Isozyme

scholarly journals Purification of chicken carbonic anhydrase isozyme-III (CA-III) and its measurement in White Leghorn chickens

2011 ◽  
Vol 53 (1) ◽  
Author(s):  
Toshiho Nishita ◽  
Yuichiro Tomita ◽  
Daisuke Yorifuji ◽  
Kensuke Orito ◽  
Hideharu Ochiai ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
White Leghorn ◽  
Carbonic Anhydrase Isozyme

scholarly journals Carbonic anhydrase isoenzymes in the erthrocytes and dorsolateral prostate of the rat

1969 ◽  
Vol 114 (3) ◽  
pp. 463-476 ◽  
Author(s):  
J. E. A. McIntosh
Keyword(s):  
Carbonic Anhydrase ◽  
High Activity ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Exchange Chromatography ◽  
Kinetic Properties ◽  
Efficient Catalyst ◽  
Molecular Weights ◽  
Hydrolysis Of ◽  
Low Activity

1. Three forms of the zinc-containing enzyme carbonic anhydrase (EC 4.2.1.1) were isolated from the erythrocytes of the rat and two forms from the dorsolateral prostate of the rat. Several additional minor components were observed but not isolated. Separation of the isoenzymes was achieved by ion-exchange chromatography, polyacrylamide-gel electrophoresis and isoelectric focusing. 2. The general properties of the isolated isoenzymes, their molecular weights and their contents of zinc were closely similar. As catalysts of the hydration of carbon dioxide, however, they were distinctly different. The two most abundant isoenzymes of the erythrocytes, which were found in equal proportions, differed 70-fold in specific activity, whereas the isoenzymes of the dorsolateral prostate were similar to one another and resembled the high-activity component of the erythrocytes. The inhibition of the latter by acetazolamide (5-acetamido-1-thia-3,4-diazole-2-sulphonamide) was mainly competitive, whereas in identical conditions the low-activity erythrocyte component and the dorsolateral prostate isoenzymes were non-competitively inhibited. 3. The use of chloroform–ethanol to remove haemoglobin from the rat haemolysate was found (a) to bring about changes in the kinetic properties of the soluble isoenzymes and (b) to cause the appearance of an additional isoenzyme. 4. The actions were compared of the inhibitors acetazolamide, 1,1-dimethylaminonaphthalene-5-sulphonamide and ethoxzolamide (6-ethoxybenzothiazole-2-sulphonamide) on the hydrolysis of p-nitrophenyl acetate catalysed by the isoenzymes. 5. The low-activity erythrocyte isoenzyme was an efficient catalyst of the hydrolysis of β-naphthyl acetate whereas the high-activity forms were much less active towards this ester. Neither of the isoenzymes present in the dorsolateral prostate catalysed this reaction. 6. Carbonic anhydrase in the rat dorsolateral prostate accounts for no more than 5% of the unusually high content of zinc in this organ.

scholarly journals Redox State and Carbonic Anhydrase Isozyme IX Expression in Human Renal Cell Carcinoma: Biochemical and Morphological Investigations

2004 ◽  
Vol 19 (3) ◽  
pp. 287-291 ◽  
Author(s):  
Sergio A. Tripodi ◽  
Maria Teresa Del Vecchio ◽  
Claudiu T. Supuran ◽  
Andrea Scozzafava ◽  
M. Gabriella Gabrielli ◽  
...  
Keyword(s):  
Renal Cell Carcinoma ◽  
Carbonic Anhydrase ◽  
Cell Carcinoma ◽  
Renal Cell ◽  
Redox State ◽  
Human Renal Cell Carcinoma ◽  
Carbonic Anhydrase Isozyme ◽  
Morphological Investigations

Localization of carbonic anhydrase in the cytoplasmic membrane of Neisseria sicca (strain 19)

1981 ◽  
Vol 27 (1) ◽  
pp. 87-92 ◽  
Author(s):  
M. N. MacLeod ◽  
I. W. DeVoe
Keyword(s):  
Carbonic Anhydrase ◽  
Density Gradient ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sucrose Density Gradient ◽  
Carbonic Anhydrase Activity ◽  
Protein Patterns ◽  
Inner Membrane ◽  
Outer Membranes ◽  
Neisseria Sicca

The carbonic anhydrase activity and the growth of Neisseria sicca 19 were inhibited by the sulfonamide acetazolamide (10−5 M). Such inhibition was completely overcome by the addition of exogenous bicarbonate. Some carbonic anhydrase activity associated with the membranous envelope fraction of the cell was released when cells were broken by sonic treatment but not during cell breakage by high-pressure extrusion. After the selective solubilization (4 °C) of the inner membrane of envelopes by treatment with 1% sodium lauroyl sarcosinate, all detectable carbonic anhydrase activity was found in the soluble (inner membrane) fraction. After fractionation of the cell envelope into inner and outer membranes by treatment with ethylenediaminetetraacetate (EDTA) followed by sucrose density gradient centrifugation, the total and specific activity of carbonic anhydrase paralleled that of succinate dehydrogenase, an inner membrane enzyme marker. The Coomassie blue stained protein patterns after polyacrylamide gel electrophoresis of the bands from the sucrose density gradient provided confirmation that the inner and outer membranes had indeed been separated.

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