Catalase in skeletal muscle fibers.
Author(s) -
K. N. Christie,
Peter J. Stoward
Publication year - 1979
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.971
H-Index - 124
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/27.4.376691
Subject(s) - catalase , hydrogen peroxide , skeletal muscle , peroxisome , endoplasmic reticulum , chemistry , skeletal muscle fibers , protein filament , biophysics , anatomy , enzyme , biochemistry , biology , gene
Catalase has been localized immunocytochemically with anti-bovine catalase in long thin filament structures in aerobic type I fibers in the skeletal muscles of normal and genetically dystrophic hamsters. The filaments range in length from 1 to 60 micron, are orientated regularly along the long axis of the fibers, and also seem to surround and project from muscle nuclei. The enzyme thus appears to be more prominent in the sarcoplasmic reticulum than in peroxisomes, and in this situation is suitably placed for destroying toxic hydrogen peroxide which may be continously generated in aerobic fibers.
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