Abstract
During the fetal and post-natal development of rat muscles, certain myosin isozymes are present which are distinct from the adult forms (380,381). The embryonic and neonatal myosins appear and disappear in an apparently sequential fashion, and, in the case of developing fast muscles, they are replaced by adult fast myosin (381). In order to study the metabolism of these proteins at the cellular level, we have prepared polyclonal antibodies to each of the developmental and adult forms and have used them in immuno-chemistry (214,511). Biochemical analyses have also been carried out, in many cases on the same muscles used for immuno cyt o chemistry, to confirm the presence of those myosins detected by the antibodies. For these analyses, electrophoresis of native myosin (402,512) is particularly well suited, since it can be performed on unfractionated muscle extracts from relatively small amounts of tissue.
Published Version
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