scholarly journals Effects of carbonic anhydrase inhibitors on contraction, intracellular pH and energy-rich phosphates of rat skeletal muscle.

1990 ◽  
Vol 423 (1) ◽  
pp. 279-297 ◽  
Author(s):  
C Geers ◽  
G Gros
2007 ◽  
Vol 36 (4) ◽  
pp. 505-514 ◽  
Author(s):  
Benoît Giannesini ◽  
Marguerite Izquierdo ◽  
Christiane Dalmasso ◽  
Yann Le Fur ◽  
Patrick J. Cozzone ◽  
...  

2001 ◽  
Vol 531 (3) ◽  
pp. 743-756 ◽  
Author(s):  
Petra Wetzel ◽  
Anke Hasse ◽  
Simon Papadopoulos ◽  
Juha Voipio ◽  
Kai Kaila ◽  
...  

1992 ◽  
Vol 294 (2) ◽  
pp. 550-556 ◽  
Author(s):  
Abdul Waheed ◽  
Xin Liang Zhu ◽  
William S. Sly ◽  
Petra Wetzel ◽  
Gerolf Gros

1986 ◽  
Vol 34 (4) ◽  
pp. 513-516 ◽  
Author(s):  
S Jeffery ◽  
N D Carter ◽  
A Smith

Specific antisera were raised against the three carbonic anhydrase (CA) isozymes, CAI, CAII, and CAIII, and were used to determine the fiber distribution of these isozymes in skeletal muscle. Fiber types were determined by ATPase staining, and the CA isozymes were detected using a peroxidase-anti-peroxidase (PAP) technique. All three isozymes were present in type I fibers; CAII and CAIII were exclusive to these fibers, and CAI were also present in some small type 2A fibers.


1991 ◽  
Vol 39 (9) ◽  
pp. 1243-1247 ◽  
Author(s):  
C D Kelly ◽  
N D Carter ◽  
P de Boer ◽  
S Jeffery ◽  
A F Moorman ◽  
...  

We carried out a variety of in situ methods of hybridization on rat liver and rat skeletal muscle using 35S-labeled or biotin-labeled rat carbonic anhydrase III (CAIII) cDNA clone. The methods were compared and evaluated. Use of the biotin system produced defined but nonspecific results which were shown not to be due to the biotinylated cDNA probe binding to the mRNA in the muscle sections. This artifact was shown to persist despite various attempts to eliminate it. Alternatively, using 35S-labeled cDNA gave reproducible results which were shown to be consistent with probe binding specifically to mRNA in the muscle section.


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