Kinetics of Enzymes with Isomechanisms: Britton Induced Transport Catalyzed by Bovine Carbonic Anhydrase II, Measured by Rapid-Flow Mass Spectrometry

1998 ◽  
Vol 352 (2) ◽  
pp. 288-292 ◽  
Author(s):  
Dexter B. Northrop ◽  
Frank.B. Simpson
Keyword(s):  
Mass Spectrometry ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Ii ◽  
Bovine Carbonic Anhydrase ◽  
Rapid Flow ◽  
Kinetics Of ◽  
Bovine Carbonic Anhydrase Ii

Extracellular carbonic anhydrase of skeletal muscle associated with the sarcolemma

1985 ◽  
Vol 59 (2) ◽  
pp. 548-558 ◽  
Author(s):  
C. Geers ◽  
G. Gros ◽  
A. Gartner
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Plasma Membranes ◽  
Oxidative Capacity ◽  
Carbonic Anhydrase Ii ◽  
Histochemical Technique ◽  
Bovine Carbonic Anhydrase ◽  
Molecular Weights ◽  
Strong Staining ◽  
Bovine Carbonic Anhydrase Ii

We report here 1) the synthesis and properties of a new macromolecular carbonic anhydrase inhibitor, Prontosil-dextran, 2) its application to determine the localization of a previously described extracellular carbonic anhydrase in skeletal muscle, and 3) the application of a recently published histochemical technique using dansylsulfonamide to the same problem. Stable macromolecular inhibitors of molecular weights of 5,000, 100,000 and 1,000,000 were produced by covalently coupling the sulfonamide Prontosil to dextrans. Their inhibition constants towards bovine carbonic anhydrase II are 1–2 X 10(-7) M. The Prontosil-dextrans, PD 5,000, PD 100,000, and PD 1,000,000, were used in studies of the washout of H14CO3-) from the perfused rabbit hindlimb. This washout is slow due to the presence of an extracellular carbonic anhydrase and can be markedly accelerated by PD 5,000 but not by PD 100,000 and PD 1,000,000. Since PD 5,000 is accessible to the entire extracellular space and PD 100,000 and PD 1,000,000 are confined to the intravascular space, we conclude that the extracellular carbonic anhydrase of skeletal muscle is located in the interstitium. The histochemical studies show a strong staining of the sarcolemma of the muscle fibers with high oxidative capacity. It appears likely, therefore, that the extracellular carbonic anhydrase of skeletal muscle is associated with muscle plasma membranes with its active site directed toward the interstitial space.

Competitive Inhibitory Effects of Acetazolamide upon Interactions with Bovine Carbonic Anhydrase II

2007 ◽  
Vol 26 (6) ◽  
pp. 371-385 ◽  
Author(s):  
Shahrokh Safarian ◽  
Fatemeh Bagheri ◽  
Ali Akbar Moosavi-Movahedi ◽  
Massoud Amanlou ◽  
Nader Sheibani
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Ii ◽  
Inhibitory Effects ◽  
Bovine Carbonic Anhydrase ◽  
Bovine Carbonic Anhydrase Ii

scholarly journals Residual Ligand Entropy in the Binding ofp-Substituted Benzenesulfonamide Ligands to Bovine Carbonic Anhydrase II

2008 ◽  
Vol 130 (37) ◽  
pp. 12420-12426 ◽  
Author(s):  
Henning Stöckmann ◽  
Agnieszka Bronowska ◽  
Neil R. Syme ◽  
Gary S. Thompson ◽  
Arnout P. Kalverda ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Ii ◽  
Bovine Carbonic Anhydrase ◽  
Bovine Carbonic Anhydrase Ii
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