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STUDIES ON MUSCLE DIFFERENTIATION. V. ANTIGENICITIES OF MYOSIN AND OF ACTIN FROM FROG SKELETAL MUSCLES 1
Author(s) -
HIRABAYASHI TAMIO,
HAYASHI YUJIRO
Publication year - 1972
Publication title -
development, growth and differentiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 66
eISSN - 1440-169X
pISSN - 0012-1592
DOI - 10.1111/j.1440-169x.1972.00133.x
Subject(s) - myosin , antigenicity , skeletal muscle , actin , biology , antiserum , antigen , meromyosin , myosin head , anatomy , microbiology and biotechnology , myosin light chain kinase , immunology
Both intact and denatured preparations of myosin and actin from frog skeletal muscles produced in rabbits antisera containing antibodies against authentic myosin and actin, respectively, though being contaminated with antibodies against other proteins. Antigenicity of our frog myosin as revealed in agar diffusion tests was indistinguishable from that of cardiac muscle myosin from the same species. Similarly, skeletal muscle myosins from other amphibians shared to a certain extent immunological characteristics with our frog myosin, but those from avian and mammalian materials did not. Similarity in antigenicity was also demonstrated among our skeletal muscle actin, cardiac muscle actin from the same species and skeletal muscle actin from the other anurans studied. However, skeletal muscle actin from an urodele could not clearly be correlated in its immunological properties with our frog actin, and those from avian and mammalian materials were antigenically different from our frog actin. Thus, the degree of antigenic similarity of these muscle proteins seemed to be correlated with the phylogenic relationship of the animals so far studied. The results also indicated that our antisera could only be applied to immuno‐cytological and immuno‐embryological studies of myosin and actin when the antisera absorbed with the corresponding antigen preparations were used as negative controls.