Muscle beta-actinin and serum albumin of the chicken are indistinguishable by physicochemical and immunological criteria.
- 1 January 1981
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 78 (1) , 74-77
- https://doi.org/10.1073/pnas.78.1.74
Abstract
Chicken muscle .beta.-actinin is considered to be 1 of the true myofibrillar components due to its specific binding to isolated myofibrils. The direct comparison of this muscle protein with serum albumin isolated from chicken, showed that they behaved identically under several electrophoretic conditions. Immunoreplica gels and double-immunodiffusion tests with antibodies prepared against .beta.-actinin established the serological identity of both proteins. No significant differences were found by circular dichroic spectroscopy or in amino acid composition. The amino-terminal sequences of the proteins were identical (H2N-Asp-Ala-Glu-His-Lys-Ser-Glu-Ile-Ala-His-Arg-Tyr-Asn-Asp-Leu-). Muscle .beta.-actinin and serum albumin apparently are similar, if not identical.This publication has 37 references indexed in Scilit:
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