The proteolytic substructure of light meromyosin. Localization of a region responsible for the low ionic strength insolubility of myosin

L. Nyitray, G. Mocz, L. Szilagyi, M. Balint, R. C. Lu, A. Wong, J. Gergely

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

Light meromyosin (LMM), prepared by limited tryptic digestions of myosin, usually contains several polypeptide chains, LMM-A, LMM-B, and LMM-C in decreasing order of molecular weight estimated from sodium dodecyl sulfate-gel electrophoresis. Further limited tryptic digestion of LMM produces well defined fragments. Fragments LF-1, LMM-D, LF-2, and LF-3 with chain masses equal to 63, 56, 47, and 30 kDa, respectively, have been isolated by column chromatography. Bas ed on time course of the changes in the sodium dodecyl sulfate-gel pattern of digests, chain masses estimated from sodium dodecyl sulfate-gel electrophoresis, and the NH2- and COOH-terminal sequences of the isolated peptides, the following scheme was deduced. The positions of the peptides along the myosin heavy chain have been established by comparison with the published primary structures of rabbit skeletal and nematode myosin. LMM and fragment LMM-D are insoluble, whereas LF-1, LF-2, and LF-3 are soluble at low ionic strength. Their solubility properties, in conjunction with their locations along the myosin heavy chain, suggest that a relatively small stretch of peptide (chain weight, 5,000 Da) located about 100 residues from the COOH terminus of myosin heavy chain is responsible for the insolubility of LMM at low ionic strength.

Original languageEnglish
Pages (from-to)13213-13220
Number of pages8
JournalJournal of Biological Chemistry
Volume258
Issue number21
Publication statusPublished - 1983

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Myosin Subfragments
Myosins
Ionic strength
Osmolar Concentration
Solubility
Myosin Heavy Chains
Sodium Dodecyl Sulfate
Peptides
Gels
Electrophoresis
Digestion
Column chromatography
Chromatography
Molecular Weight
Molecular weight
Rabbits
Weights and Measures

ASJC Scopus subject areas

  • Biochemistry

Cite this

The proteolytic substructure of light meromyosin. Localization of a region responsible for the low ionic strength insolubility of myosin. / Nyitray, L.; Mocz, G.; Szilagyi, L.; Balint, M.; Lu, R. C.; Wong, A.; Gergely, J.

In: Journal of Biological Chemistry, Vol. 258, No. 21, 1983, p. 13213-13220.

Research output: Contribution to journalArticle

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T1 - The proteolytic substructure of light meromyosin. Localization of a region responsible for the low ionic strength insolubility of myosin

AU - Nyitray, L.

AU - Mocz, G.

AU - Szilagyi, L.

AU - Balint, M.

AU - Lu, R. C.

AU - Wong, A.

AU - Gergely, J.

PY - 1983

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AB - Light meromyosin (LMM), prepared by limited tryptic digestions of myosin, usually contains several polypeptide chains, LMM-A, LMM-B, and LMM-C in decreasing order of molecular weight estimated from sodium dodecyl sulfate-gel electrophoresis. Further limited tryptic digestion of LMM produces well defined fragments. Fragments LF-1, LMM-D, LF-2, and LF-3 with chain masses equal to 63, 56, 47, and 30 kDa, respectively, have been isolated by column chromatography. Bas ed on time course of the changes in the sodium dodecyl sulfate-gel pattern of digests, chain masses estimated from sodium dodecyl sulfate-gel electrophoresis, and the NH2- and COOH-terminal sequences of the isolated peptides, the following scheme was deduced. The positions of the peptides along the myosin heavy chain have been established by comparison with the published primary structures of rabbit skeletal and nematode myosin. LMM and fragment LMM-D are insoluble, whereas LF-1, LF-2, and LF-3 are soluble at low ionic strength. Their solubility properties, in conjunction with their locations along the myosin heavy chain, suggest that a relatively small stretch of peptide (chain weight, 5,000 Da) located about 100 residues from the COOH terminus of myosin heavy chain is responsible for the insolubility of LMM at low ionic strength.

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