Biomedical subjects

T Obinata

Publications and source records attributed to T Obinata.

4 recordsLinked to original sources

PubMed1979

Crystalloids of actin-like filaments in the Sertoli cell of the swine testis.

Normal swine testes, congenital cryptorchid swine testes, and normal human tests were exposed to HMM (heavy meromyosin) after either glycerination or saponin treatment in order to determine whether the fine filaments composing the crystalloids in the Sertoli cells of the cryptorchid swine testes bind HMM to form arrowhead complexes. Short bundles of microfilaments observed in the basal part of the Sertoli cells in both normal and cryptorchid testes also bind HMM. Similar bundles of HMM-bound filaments are observed in the vicinity of spermatocytes. The periodicity of the arrowhead complexes is about 35 nm, and all arrowheads on a given filament point in the same direction. In addition, the polarity of the HMM-bound filaments in a given crystalloid or bundle is uni-directional. A mechanism for the formation of the swine crystalloids has been strongly support this hypothesis. Fine filaments of Charcot-Boettcher's crystalloid in human Sertoli cells did not bind HMM. Therefore the fine filaments of the human crystalloid are not actin-like in nature.

Actins↗

PubMed1979

Troponin in embryonic chick skeletal muscle cells in vitro. An immunoelectron microscope study.

The fine structurel distribution of troponin on thin filaments in developing myofibrils was investigated by the use of immunoelectron microscopy. Embryonic chick skeletal muscle cells grown in vitro were treated with antibodies against each of the troponin components (troponin T, I, and C) from adult chicken muscles. Each antibody was distributed along the thin filaments with a period of 38 nm. It is concluded that these newly synthesized regulatory proteins are assembled at their characteristic position from the initial phases of myofibrillogenesis.

Animals↗

PubMed1979

Immunochemical comparison of myosin light chains from chicken fast white, slow red, and cardiac muscle.

Antibodies were formed against the myosin light chains isolated from chicken fast skeletal, slow skeletal, and cardiac muscle and the antigenicities of the light chains were compared by double immunodiffusion and immunoelectrophoresis. It was shown that fast light chains are immunologically different from light chains of slow and cardiac myosin, while the slow and cardiac muscle light chains have similar immunological characteristics; that is, the light chains of apparent molecular weight about 27,000 daltons in SDS-acrylamide gel electrophoresis of slow and cardiac muscle are immunologically indistinguishable, and the other light chains of apparent molecular weight about 19,000 daltons of both muscles include a common antigenic site.

Animals↗

PubMed1977

Polarity of actin filaments at the initial stage of myofibril assembly in myogenic cells in vitro.

The polarity of thin filaments in relation to thick filaments in developing muscle cells in vitro was investigated. The majority of thin filaments exhibited the right polarity and spatial position similar to that seen in mature myofibrils. It appears that the interaction between thick and thin filaments exists in the initial phases of myofibrillogenesis. Cortical microfilaments are found to have their polarities arranged randomly.

Actins↗