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Biomedical subjects

E Damiani

Publications and source records attributed to E Damiani.

80 records · Page 5Linked to original sources
PubMed1982

Fast to slow change of myosin in nemaline myopathy: electrophoretic and immunologic evidence.

Muscle biopsies from two familial and one sporadic case with congenital nemaline myopathy and seven healthy family members were examined for myosin composition. Myosin was characterized with respect to light chain (LC) composition by one-dimensional and two-dimensional electrophoresis, and by immunologic methods (enzyme-linked immunosorbent assay [ELISA]), using specific antibody for rabbit fast myosin LCl (LC1F). Type I fiber predominance was associated with the substitution of a hybrid, predominantly "slow" to a virtually pure "slow" myosin LC pattern for the "mixed" pattern found with myosin of normal muscle. Muscle myosin from the relatives had apparently normal light chain composition.

Adult↗
PubMed1981

Polymorphism of sarcoplasmic-reticulum adenosine triphosphatase of rabbit skeletal muscle.

Antibody was raised in chickens against purified sarcoplasmic-reticulum Ca2+-activated ATPase (Ca2+-ATPase). The immunological relationship between the Ca2+-ATPase of fast-muscle and slow-muscle sarcoplasmic reticulum was investigated by a one-step and a two-step competitive enzyme-linked immunosorbent assay (ELISA). The results show marked antigenic differences between the membrane-bound Ca2+-ATPase of the sarcoplasmic-reticulum vesicles from fast muscle and slow muscle, beside differences in the membrane content of ATPase protein.

Animals↗
PubMed1981

Characterization of human muscle myosins with respect to the light chains.

Isolated myosins from human predominantly fast and slow muscles, human neonatal and foetal muscle were examined for light chain composition by one- and two-dimensional electrophoresis. The LC1F, LC2F and LC3F light chains were identical with their counterparts from rabbit fast myosin. Human LC1S was identified by correlative criteria as a single component having a molecular weight slightly lower than, but an electric charge similar to, that of rabbit LC1Sb. Consequently, human LC1S appears to be much less heterogeneous relative to LC1F than is the case with other mammalian species. A high immunological cross-reactivity was likewise observed, with antibody specific to rabbit LC1F, between the isolated myosins from several human mixed muscles and rabbit fast myosin, though reactivity was highest with foetal myosin (having a pure-fast-light-chain pattern).

Animals↗
PubMed1981

Enzyme-linked immunoassay for study of sarcoplasmic reticulum adenosine triphosphatase.

The immunological reactivity of isolated sarcoplasmic reticulum from rabbit fast muscle was tested with antibody to the Ca2+-pump protein which is the predominant component of these membranes. Microplate enzyme-linked immunoassay (ELISA) gave highly reproducible results under the conventional conditions used for checkerboard titration of soluble antigens and antibody. Parallel electron microscope observation of the incubated SR vesicles, negatively stained with ammonium molybdate, shows that the immunologically reactive form of the Ca2+-pump protein is still present in membrane-bound form.

Adenosine Triphosphatases↗