Muscle beta-actinin and serum albumin of the chicken are indistinguishable by physicochemical and immunological criteria.

Abstract

Chicken muscle beta-actinin is considered to be one of the "true" myofibrillar components due to its specific binding to isolated myofibrils. Surprisingly, the direct comparison of this muscle protein with serum albumin, both isolated from chicken, showed that they behaved identically under several electrophoretic conditions. Furthermore, 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. In addition, the amino-terminal sequences of both proteins were identical (H2N-Asp-Ala-Glu-His-Lys-Ser-Glu-Ile-Ala-His-Arg-Tyr-Asn-Asp-Leu-). Combined, these results strongly indicate that muscle beta-actinin and serum albumin are similar, if not identical.

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