Many studies have established a correlation of differences in the activities of various muscle types with differences in the expression of myosin isoforms. In this paper we report the sequence determination of myosin light chain-2 from rabbit slow skeletal (LC2s) and ventricular (LC2v) nmscles. We sequenced tryptic peptides from LC2v which account for all except a few terminal amino acid residues. The major part (87 residues) of the rabbit LC2s sequence, obtained from tryptic and cyanogen bromide (CNBr) peptides, was found to be identical to rabbit LC2v. Our results provide the first sequence information on LC2s from any species, and lend strong support to the hypothesis that LC2s and LC2v are identical. Comparisons of rabbit LC2v and LC2s with rabbit LC2f (from fast skeletal muscle), and also with chicken LC2f and LC2v, show clearly that LC2s and LC2v from mammalian and avian species are more closely related to each other than they are to LC2f isoforms from the same species.
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July 01 1986
Amino acid sequence of rabbit ventricular myosin light chain-2: Identity with the slow skeletal muscle isoform
John H. Collins;
John H. Collins
1Department of Biology, Clarkson University, Potsdam, New York 13676, USA
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Janet L. Theibert;
Janet L. Theibert
1Department of Biology, Clarkson University, Potsdam, New York 13676, USA
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Luciano Dalla Libera
Luciano Dalla Libera
2C.N.R. Unit for Muscle Biology and Physiopathology, Institute of General Pathology, University of Padova, Via Loredan 16, 35100 Padova, Italy
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Publisher: Portland Press Ltd
Received:
July 16 1986
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1986 Plenum Publishing Corporation
1986
Biosci Rep (1986) 6 (7): 655–661.
Article history
Received:
July 16 1986
Citation
John H. Collins, Janet L. Theibert, Luciano Dalla Libera; Amino acid sequence of rabbit ventricular myosin light chain-2: Identity with the slow skeletal muscle isoform. Biosci Rep 1 July 1986; 6 (7): 655–661. doi: https://doi.org/10.1007/BF01114760
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