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Localization of myoglobin in human muscle cells by immunoelectron microscopy
Author(s) -
Kawai Hisaomi,
Nishino Hiroshi,
Nishida Yoshihiko,
Masuda Kenjiro,
Saito Shiro
Publication year - 1987
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880100207
Subject(s) - immunoelectron microscopy , myoglobin , immunoperoxidase , horseradish peroxidase , skeletal muscle , chemistry , immunogold labelling , electron microscope , anatomy , biophysics , pathology , biology , ultrastructure , biochemistry , immunohistochemistry , medicine , monoclonal antibody , antibody , physics , optics , immunology , enzyme
The localization of myoglobin in human skeletal muscle cell was studied by immunoelectron microscopy. The Fab'‐horseradish peroxidase (HRP) conjugate was prepared by the maleimide method recently developed by Ishikawa et al. This method gave better recovery and less polymerization of HRP than the periodate method. By the direct immunoperoxidase method using this conjugate, myoglobin was shown to be localized in the I‐band region of skeletal muscle cells. The outer membrane of mitochondria and triads stained intensely, but A‐bands were not stained. Myonuclei and intermyofibrillar spaces were also not stained. The localization of myoglobin in the I‐band implies its function in energy generation.