A 26K fragment of troponin T from rabbit skeletal muscle.

Abstract:

:A 26K fragment of troponin T, which was produced by endogenous proteases in rabbit skeletal muscle, was isolated by SE-Sephadex column chromatography. This fragment sensitized both superprecipitation and ATPase of actomyosin to calcium ions, to the same extent as troponin T. There was no difference in affinity for tropomyosin between this fragment and troponin T as examined by affinity chromatography. Amino acid analysis showed that this fragment consisted of residues Ala-46-Lys-259 of troponin T. The N-terminal 45 residues of troponin T, therefore, are not essential for the physiological action of troponin T. It was also observed that Ca2+-activated neutral protease digested troponin T into the 26K fragment in the native thin filament, while the protease digested troponin T in a different way in the reconstituted thin filament.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Ohtsuki I,Shiraishi F,Suenaga N,Miyata T,Tanokura M

doi

10.1093/oxfordjournals.jbchem.a134740

subject

Has Abstract

pub_date

1984-05-01 00:00:00

pages

1337-42

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

95

pub_type

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