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PubMed · 7887920

Temperature acclimation induces light meromyosin isoforms with different primary structures in carp fast skeletal muscle.

S Watabe·J Imai·M Nakaya·Y Hirayama·Y Okamoto·H Masaki·T Uozumi·I Hirono·T Aoki
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Abstract

Carp acclimated to 10 degrees C gave 69k, 66k, and 62kDa light meromyosin (LMM) fragments in SDS-PAGE, while fish acclimated to 30 degrees C gave 74k, 69k, 66k, and 62kDa fragments. The microsequence analysis revealed that the 69k and 66kDa components from the 10 degrees C-acclimated carp contained an N-terminal amino acid sequence different from that of 62kDa. The four fragments from the 30 degrees C-acclimated carp showed the same sequence as that of the 69k and 66kDa components from the 10 degrees C-acclimated carp, except that the 2nd amino acid, Ala, of the 10 degrees C-acclimated LMM was replaced by Thr. DNA fragments encoding an N-terminal region of LMM were amplified by PCR or reverse transcriptase-PCR, demonstrating that the two acclimated groups further contained several amino acids substituted.

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AcclimatizationAmino Acid SequenceAnimalsCarpsChickensCloning, MolecularCold TemperatureDNA, ComplementaryElectrophoresis, Polyacrylamide GelHumansMiceMolecular Sequence DataMuscle Fibers, Fast-TwitchMuscle, SkeletalMyosin SubfragmentsPeptide FragmentsRNA, MessengerRabbitsRatsRecombinant ProteinsSequence Homology, Amino AcidTemperatureComparative StudyJournal ArticleResearch Support, Non-U.S. Gov't

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S Watabe, J Imai, M Nakaya, Y Hirayama, Y Okamoto, H Masaki, T Uozumi, I Hirono, T Aoki. 1995-03-08. Temperature acclimation induces light meromyosin isoforms with different primary structures in carp fast skeletal muscle.. https://doi.org/10.1006/bbrc.1995.1313

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