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PMID: 4008630 Published · ppublish English Journal Article

Angle of active site of myosin heads in contracting muscle during sudden length changes.

Journal of muscle research and cell motility ·Vol. 6 ·No. 1 ·1985-02-00 ·Pages 43-52

Yanagida T

Abstract

The change in orientation of myosin crossbridges in contracting muscle during sudden length changes was examined by fluorescence polarization. This study used a fluorescent ATP analogue, 1,N6-etheno-2-aza-ATP(epsilon-2-aza-ATP) as a probe. Its fluorescence is considerably enhanced upon binding with myosin and is dependent on the chemical state of the myosin-nucleotide complex in muscle. The results showed that nucleotides bound to crossbridges in the intermediate attached state (presumably AM-epsilon-2-aza-ADP-Pi) during isometric contraction are highly oriented at the same angle as that of AM in rigor with bound epsilon-2-aza-ADP. Furthermore the orientation of nucleotides bound to crossbridges in the attached state is not altered during sudden changes in length of isometrically contracting muscle. The results of this time-resolved measurement support the conclusion obtained from a previous steady-state experiment that change in axial orientation of the active site of the myosin head is not involved in force generation.

MeSH Terms
Animals Binding Sites Calcium/pharmacology Ethenoadenosine Triphosphate/analogs & derivatives,pharmacology Isometric Contraction/drug effects Kinetics Muscle Contraction/drug effects Muscle Relaxation/drug effects Muscles/physiology Myosins/metabolism Rabbits Spectrometry, Fluorescence
Chemicals
Ethenoadenosine Triphosphate aza-epsilon-ATP Myosins Calcium
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Yanagida T
References (19)
19 references, click to expand
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Article Info
Journal
Journal of muscle research and cell motility
Abbr.
J Muscle Res Cell Motil
ISSN
0142-4319
DOI
10.1007/BF00712310
Published
1985-02-00
Pages
43-52
Language
English
Region
Netherlands
NLM ID
8006298
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00712310 View journal details
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