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Light Meromyosin
Known as:
Meromyosin, Light
, Myosin Rod
National Institutes of Health
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Related topics
1 relation
Broader (1)
Myosin Subfragments
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2001
2001
Insolubility-determining Reg on in Light
L. Nyitray
,
G. Mocz
,
+4 authors
J. Gergely
2001
Corpus ID: 44574770
Light meromyosin (LMM), prepared by limited tryptic digestion of myosin, usually contains several polypeptide chains, LMM-A, LMM…
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2001
2001
Bending of smooth muscle
A. R.
2001
Corpus ID: 5128637
Electron microscopy of mammalian smooth muscle myosin rods showed them to be 153 f 7 nm (SD) long, and to bend sharply (> 90…
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1997
1997
The 66 k-Da protein identified as a light meromyosin is involved in the setting of surimi
A. Alam
,
E. Niwa
1997
Corpus ID: 31518227
The 66 kilo-Dalton (k-Da) protein split off from the cross linked myosin heavy chain (CMHC) formed due to the setting of Alaska…
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1984
1984
Tryptic digestion of rabbit skeletal myofibrils: an enzymatic probe of myosin cross-bridges.
Theresa Chen
,
Emil Reisler
Biochemistry
1984
Corpus ID: 42694592
Tryptic digestion of rabbit skeletal myofibrils under physiological ionic strength and pH conditions was used as a probe of cross…
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1981
1981
[Secondary structure and amino acid composition of protein complex associated with the rod part of myosin molecule].
A. M. Arutiunian
,
I. Bolotina
,
M. Kalamkarova
,
E. Kofman
,
V. I. Lugauskas
Biofizika
1981
Corpus ID: 39124489
The secondary structure and amino acid composition of a protein complex (LMM-Rp) bound to the heavy chains (HC) of light…
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Highly Cited
1977
Highly Cited
1977
Fluorescence depolarization studies on the flexibility of myosin rod.
Stephen C. Harvey
,
Herbert C. Cheung
Biochemistry
1977
Corpus ID: 20205351
The single photon counting method has been used to measure the decay of fluorescence polarization anisotropy of myosin rods…
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1975
1975
Thermal transitions of myosin and its helical fragments. I. Shifts in proton equilibria accompanying unfolding.
C. C. Goodno
,
C. Swenson
Biochemistry
1975
Corpus ID: 44679522
The thermal transitions of myosin and its helical fragments have been studied with pH as the observable. Heating unbuffered…
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