Carbonic anhydrase levels in blue-green algae

1975 ◽  
Vol 53 (20) ◽  
pp. 2385-2387 ◽  
Author(s):  
R. K. Ingle ◽  
Brian Colman
Keyword(s):  
Enzyme Activity ◽  
Carbonic Anhydrase ◽  
Green Algae ◽  
Carbonic Anhydrase Activity ◽  
Anacystis Nidulans ◽  
Blue Green Algae ◽  
Membrane Bound

Carbonic anhydrase (carbonate dehydratase, EC 4.2.1.1) activity was detected in four species of blue-green algae, Anabaena flos-aquae, Anacystis nidulans, Coccochloris peniocystis, and Oscillatoria sp., grown with air, but no significant enzyme activity was detected in these algae when grown with 5% CO2 in air. The enzyme was found not to be membrane-bound, was inhibited by 1 mM Diamox, and had an apparent Km of 15.6 mM. Carbonic anhydrase activity in all four blue-green algae was significantly lower than that reported for unicellular green algae.

Carbonic anhydrase distribution in rodent embryos and its relationship to acetazolamide teratogenesis.

1981 ◽  
Vol 29 (10) ◽  
pp. 1213-1218 ◽  
Author(s):  
C M Schreiner ◽  
K S Hirsch ◽  
W J Scott
Keyword(s):  
Enzyme Activity ◽  
Carbonic Anhydrase ◽  
Staining Pattern ◽  
Carbonic Anhydrase Activity ◽  
Primary Site ◽  
Mouse Embryos ◽  
Histochemical Method ◽  
Site Of Action ◽  
Activity Form ◽  
Low Activity

The carbonic anhydrase inhibitor, acetazolamide, leads to a unique distal postaxial right forelimb deformity in rats and CBA/J mice, but SWV mice are completely resistant. Using Hansson's histochemical method, the distribution of carbonic anhydrase and its inhibition by acetazolamide in rat, CBA/J mouse, and SWV mouse embryos were compared. Carbonic anhydrase activity was demonstrable in many tissues of sensitive rat and CBA/J mouse embryos and in resistant SWV mouse embryos. The forelimb buds of resistant and sensitive embryos possess carbonic anhydrase activity in the area between the ectoderm and adjacent mesenchyma with no localization of enzyme activity corresponding to the malformation seen in acetazolamide teratogenesis. This suggests that carbonic anhydrase in the forelimbs is not the primary site of action for acetazolamide. A distinctive staining pattern of nucleated erythrocytes in resistant embryos indicated the presence of a low activity form of carbonic anhydrase in nearly half of the erythrocytes. A five-to tenfold greater amount of acetazolamide was needed to completely inhibit carbonic anhydrase activity in nucleated erythrocytes from resistant embryos than in those from sensitive embryos. The existence of a low activity form of carbonic anhydrase in SWV embryo erythrocytes may be the basis of resistance to acetazolamide teratogenesis.

Effects of High Boron Concentrations on Nitrate Utilization and Photosynthesis in Blue-green Algae Anabaena PCC 7119 and Anacystis nidulans

1987 ◽  
Vol 128 (1-2) ◽  
pp. 161-168 ◽  
Author(s):  
P. Mateo ◽  
F. Martínez ◽  
I. Bonilla ◽  
E. Fernandez Valiente ◽  
E. Sanchez Maeso
Keyword(s):  
Green Algae ◽  
Anacystis Nidulans ◽  
Blue Green Algae ◽  
High Boron

Plasma membrane-bound carbonic anhydrase activity in the regenerating rat liver

1991 ◽  
Vol 1061 (1) ◽  
pp. 9-14 ◽  
Author(s):  
Jose Juan García Marín ◽  
Arancha Tabernero Urbieta ◽  
Fernando Pérez Barriocanal ◽  
Emilio Rodríguez Barbero ◽  
Nelida Eleno
Keyword(s):  
Plasma Membrane ◽  
Carbonic Anhydrase ◽  
Rat Liver ◽  
Carbonic Anhydrase Activity ◽  
Regenerating Rat Liver ◽  
Membrane Bound

Rat lung carbonic anhydrase: activity, localization, and isozymes

1986 ◽  
Vol 60 (2) ◽  
pp. 638-645 ◽  
Author(s):  
R. P. Henry ◽  
S. J. Dodgson ◽  
R. E. Forster ◽  
B. T. Storey
Keyword(s):  
Enzyme Activity ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Activity ◽  
Hydration Reaction ◽  
Rat Lung ◽  
Cell Debris ◽  
Blood Contamination ◽  
Total Enzyme Activity ◽  
Erythrocyte Lysis ◽  
A Cell

sCarbonic anhydrase activity in rat lungs perfused free of blood was localized by homogenization of the tissue followed by differential centrifugation. Four fractions were obtained from the homogenate, a cell debris pellet with a mitochondrial pellet and a microsomal pellet with a clear cytosol supernatant. The last named fraction contained 67% of the total enzyme activity; the cell debris contained 18%, and the mitochondrial and microsomal contained 8 and 7%, respectively. Of the 33% of enzyme activity associated with the pellet fraction, 25% could be experimentally defined as membrane associated by its solubilization with 0.3 M tris-(hydroxymethyl) aminoethane sulfate buffer. The remainder was defined as membrane bound. Purification of the soluble carbonic anhydrase from the lung yielded two isozymes with electrophoretic and inhibitor sensitivities apparently identical with the blood isozymes. Hemoglobin analysis showed that the lung isozymes could not have included more than 0.03% enzyme from blood contamination. The carbonic anhydrase activity present in the whole rat lung would give an average acceleration of the CO2 hydration reaction under physiological conditions over the uncatalyzed rate of 122, sufficient to maintain equilibration between CO2 and plasma HCO3- during blood transit of the lung. If the membrane-associated activity is mostly on the plasma membrane of the endothelial cells and available to the capillary blood, it would be sufficient to give this acceleration. We suggest that the possible source of this membrane-associated activity might be adsorption from the blood of carbonic anhydrase liberated by erythrocyte lysis.

Renal carbonic anhydrase

1982 ◽  
Vol 243 (4) ◽  
pp. F311-F324 ◽  
Author(s):  
D. C. Dobyan ◽  
R. E. Bulger
Keyword(s):  
Carbonic Anhydrase ◽  
Collecting Duct ◽  
Mammalian Species ◽  
Carbonic Anhydrase Activity ◽  
The Body ◽  
Carbonic Anhydrases ◽  
Duct System ◽  
Renal Carbonic Anhydrase ◽  
Membrane Bound ◽  
Editorial Review

Carbonic anhydrase is a zinc metalloenzyme widely distributed throughout the tissues of the body. This enzyme exists in a number of isozymic forms in most mammalian species. Significant advances over the past decade have been made in characterizing the nature of renal carbonic anhydrase. In the kidney, this enzyme is thought to play a pivotal role in urinary acidification and bicarbonate reabsorption. Two distinct isozymes of carbonic anhydrase have now been identified in the mammalian kidney. A soluble cytoplasmic form, similar if not identical to human erythrocyte carbonic anhydrase C, accounts for the bulk of the renal carbonic anhydrase activity. In addition, a membrane-bound form constituting only about 2--5% of the renal activity has been found in the brush border and basolateral fractions of kidney homogenates. The histochemical and immunocytochemical localization of these isozymes along the nephron and collecting duct system of various mammalian species suggests that marked heterogeneity exists. The Editorial Review examines the biochemical and morphological approaches that have been used to elucidate the nature of renal carbonic anhydrase and to assess its distribution along the urinary tubule. Possible physiological roles for the renal carbonic anhydrases are considered for the different segments of the nephron and collecting duct system.

A micromethod for measuring carbonic anhydrase activity using 18O exchange between CO2 and H2O

1988 ◽  
Vol 65 (4) ◽  
pp. 1902-1906 ◽  
Author(s):  
N. Bitterman ◽  
L. Lin ◽  
R. E. Forster
Keyword(s):  
Enzyme Activity ◽  
Carbonic Anhydrase ◽  
High Activity ◽  
Intact Cell ◽  
Porous Membrane ◽  
Carbonic Anhydrase Activity ◽  
Published Data ◽  
Hydration Reaction ◽  
Activity Type ◽  
Reaction Velocity

We have developed a method of measuring the activity and characteristics of carbonic anhydrase (CA) using the disappearance of 18O from CO2 in 1 ml of gas contained in a glass chamber as it exchanges with H2O in 0.01 ml 0.25 M NaHCO3 solution in a thin (25 micron) porous membrane. Serial gas samples (approximately 0.02 ml) are analyzed in a mass spectrometer to obtain the rate of disappearance of the label. The enzyme activity can be measured inside intact cell or particle membranes. As little as 10(-15) mol of high-activity type CA can be detected at 25 degrees C, and the activity of 200 times this amount can be measured. The uncatalyzed hydration reaction velocity constant was 0.056 +/- 0.004 s-1, in agreement with published data.

Cellular Effects of Herbicide Simazine on Blue-Green Algae

1982 ◽  
Vol 40 ◽  
pp. 324-325
Author(s):  
R.S. Mehta ◽  
K.W. Hawxby
Keyword(s):  
Green Algae ◽  
Green Alga ◽  
Anacystis Nidulans ◽  
Blue Green Alga ◽  
Blue Green Algae ◽  
Cellular Effects

This study is sought to compare the effects of herbicide simazine (2-chloro 4,-6-bis (ethylamino)-S-triazine) on cellular corrponents of control and the treated cells of the blue-green alga (cyanobacterium) Anacystis nidulans, which are well defined and documented. The extent to which this initial interpretation of observations are realities, must be determined by biochemical and perhaps cytochemical techniques as well.

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