Human Skeletal Muscle Proteins. The Primary Structure of Troponin C

Overview

Journal J Mol Evol

Specialty Biochemistry

Date 1976 Oct 27

PMID 978749

Citations 9

Authors

O Castillo

H Lehmann

Affiliations

Soon will be listed here.

Abstract

The primary structure of the major component of human skeletal muscle troponin C has been established. The troponin C was purified by ammonium sulphate and isoelectric fractionation, followed by two chromatographic steps on DEAE Sephadex. The sequence was determined from the different overlapping enzymic peptides and by dansyl-Edman degradation. The only difference between rabbit skeletal muscle troponin C and the major component of human skeletal troponin C was found at position 112: Ala (rabbit), Pro (human). The partial amino acid sequence of the first 86 residues of the minor component of human skeletal troponin C was found to resemble the troponin C from bovine cardiac muscle. The only difference between them, has tentatively been located at position 62: Glu (human), Asp (bovine). These similarities suggest that troponin C is, from the point of view of molecular, one of the most conservative proteins so far studied.

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