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.

[1]  H. Hofer,et al.  Metabolic heterogeneity of muscle fibers classified by myosin ATPase , 1979, Histochemistry.

[2]  T. Kumpulainen.  Immunohistochemical localization of human carbonic anhydrase isoenzyme C , 1979, Histochemistry.

[3]  T. Kumpulainen,et al.  Immunohistochemical demonstration of carbonic anhydrase , 1978, Histochemistry.

[4]  G. Lonnerholm.  Carbonic anhydrase in rat liver and rabbit skeletal muscle: further evidence for the specificity of the histochemical cobalt-phosphate method of Hansson. , 1980 .

[5]  S. Spicer,et al.  The immunohistolocalization of carbonic anhydrase in rodent tissues. , 1979, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[6]  E. Noltmann,et al.  Discovery of carbonic anhydrase in rabbit skeletal muscle and evidence for its identity with "basic muscle protein". , 1978, The Journal of biological chemistry.

[7]  J. Moynihan.  Carbonic anhydrase activity in mammalian skeletal and cardiac muscle. , 1977, The Biochemical journal.

[8]  M. A. Khan.  Histochemical characteristics of vertebrate striated muscle: a review. , 1976, Progress in histochemistry and cytochemistry.

[9]  M. J. Carter,et al.  CARBONIC ANHYDRASE:ISOENZYMES. PROPERTIES. DISTRIBUTION. AND FUNCTIONAL SIGNIFICANCE , 1972, Biological reviews of the Cambridge Philosophical Society.

[10]  M. Brooke,et al.  Muscle fiber types: how many and what kind? , 1970, Archives of neurology.

[11]  L. Guth,et al.  Procedure for the histochemical demonstration of actomyosin ATPase. , 1970, Experimental neurology.

[12]  T. Maren,et al.  Carbonic anhydrase: chemistry, physiology, and inhibition. , 1967, Physiological reviews.