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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

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

doi

10.1006/bbrc.1995.1313

subject

Has Abstract

pub_date

1995-03-08 00:00:00

pages

118-25

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X85713137

journal_volume

208

pub_type

杂志文章

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