Carbonic anhydrase in the type I skeletal muscle fibers of the rat. An immunohistochemical study.
The localization of carbonic anhydrase (CA) was studied in rat skeletal muscles with the use of immunohistochemical (peroxidase-antiperoxidase) method. CA was observed in all those fibers that also showed pH 4.3 stable actomyosin adenosine triphosphatase activity (type I fibers), but the reverse did not necessarily hold. More specifically, CA was apparently localized in I-bands, and a weak reaction was also observed in sarcolemma. The function of CA in muscle fibers is possibly connected with the greater demands on CO2 transport and buffer system in muscles adapted to long-lasting contractions.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D002256:Carbonic Anhydrases / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D007124:Immunoenzyme Techniques; D008297:Male; D009132:Muscles / Q000201:enzymology*; D009210:Myofibrils / Q000201:enzymology; D051381:Rats; D012508:Sarcolemma / Q000201:enzymology
D000251:Adenosine Triphosphatases; D002256:Carbonic Anhydrases