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Thermal denaturation of the alkali light chain‐20 kDa fragment complex obtained from myosin subfragment 1
Author(s) -
Nina L. Golitsina,
Valery L. Shnyrov,
Dmitrii I. Levitsky
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80532-l
Subject(s) - myosin , denaturation (fissile materials) , differential scanning calorimetry , chemistry , immunoglobulin light chain , skeletal muscle , alkali metal , chain (unit) , biochemistry , organic chemistry , biology , thermodynamics , nuclear chemistry , physics , antibody , astronomy , immunology , endocrinology
The thermal denaturation of the myosin subfragment 1 (S1) from rabbit skeletal muscle and of its derivatives obtained by tryptic digestion has been studied by means of differential scanning calorimetry. Two distinct thermal transitions were revealed in the isolated complex of the C‐terminal 20 kDa fragment of the S1 heavy chain with the alkali light chain. These transitions were identified by means of a thermal gel analysis method. It has been shown that the thermal denaturation of the 20 kDa fragment of the S1 heavy chain correlates with the melting of the most thermostable domain in the S1 molecule. It is concluded that this domain is located in the C‐terminal 20 kDa segment of the S1 heavy chain.