Thermal unfolding of homodimers and heterodimers of different skeletal-muscle isoforms of tropomyosin

2018 ◽  
Vol 243 ◽  
pp. 1-7 ◽  
Author(s):  
Alexander M. Matyushenko ◽  
Sergey Y. Kleymenov ◽  
Denis S. Susorov ◽  
Dmitrii I. Levitsky
Keyword(s):  
Skeletal Muscle ◽  
Thermal Unfolding ◽  
Muscle Isoforms

Thermal unfolding of various human non-muscle isoforms of tropomyosin

2019 ◽  
Vol 514 (3) ◽  
pp. 613-617 ◽  
Author(s):  
Victoria V. Nefedova ◽  
Marina A. Marchenko ◽  
Sergey Y. Kleymenov ◽  
Petr N. Datskevich ◽  
Dmitrii I. Levitsky ◽  
...  
Keyword(s):  
Thermal Unfolding ◽  
Muscle Isoforms

Thermal unfolding of Acanthamoeba myosin II and skeletal muscle myosin

1996 ◽  
Vol 59 (3) ◽  
pp. 365-371 ◽  
Author(s):  
Michal Zolkiewski ◽  
M.Jolanta Redowicz ◽  
Edward D. Korn ◽  
Ann Ginsburg
Keyword(s):  
Skeletal Muscle ◽  
Myosin Ii ◽  
Thermal Unfolding ◽  
Skeletal Muscle Myosin ◽  
Muscle Myosin

Thermal unfolding of monomeric Ca(II),Mg(II)-ATPase from sarcoplasmic reticulum of rabbit skeletal muscle

FEBS Letters ◽  
1994 ◽  
Vol 343 (2) ◽  
pp. 155-159 ◽  
Author(s):  
Jaime M. Merino ◽  
Jesper V. Moller ◽  
Carlos Gutiérrez-Merino
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Rabbit Skeletal Muscle ◽  
Thermal Unfolding

scholarly journals Protease-susceptible sites and properties of fragments of aortic smooth-muscle myosin

1995 ◽  
Vol 312 (2) ◽  
pp. 511-518 ◽  
Author(s):  
L King ◽  
M J Jiang ◽  
T S Huang ◽  
G C Sheu
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Ionic Strength ◽  
Molecular Mass ◽  
Thermal Unfolding ◽  
Aortic Smooth Muscle ◽  
Dramatic Difference ◽  
Low Ionic Strength ◽  
Muscle Myosin ◽  
Myosin Rod

We have examined the protease susceptibility of aortic myosin, the thermal unfolding profiles of myosin rod and light meromyosin (LMM) and the solubility properties of the LMM fragments. Two major protease-susceptible sites were found, located at the head-rod junction and the heavy meromyosin (HMM)-LMM junction. Both tryptic and chymotryptic digestion of aortic myosin rod produced the LMM (80-85 kDa) and short subfragment 2 (S-2) (40-45 kDa) segments, which were similar to those of gizzard myosin rod and differed from the short LMM (70 kDa) and long S-2 (58 kDa) segments produced from skeletal-muscle rod. The thermal unfolding profile of aortic myosin rods exhibited three helix-unfolding transitions, at 47.5, 51 and 54 degrees C, similar to those of gizzard rods yet different from those of skeletal-muscle rods. There was a dramatic difference in the solubility of aortic LMM fragments of various molecular mass, as for gizzard smooth-muscle LMM and rabbit skeletal-muscle LMM. LMM fragments of molecular mass 77 kDa or more were completely insoluble in low-ionic-strength buffer, whereas LMM fragments of molecular mass 73 kDa or less were completely soluble in low-ionic-strength buffer. Proteolytic digestion patterns of LMM showed two additional protease-susceptible sites located 13 and 30 kDa from the ends of the LMM molecule. This suggests the existence of flexible regions within the LMM molecule, which may be responsible for the folded form of aortic myosin.

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