Affinity for MgADP and force of unbinding from actin of myosin purified from tonic and phasic smooth muscle

American Journal of Physiology - Cell Physiology

Volumn 295, Issue 3, 2008, Pages

  Léguillette, Renaud ^a   Zitouni, Nedjma B ^a   Govindaraju, Karuthapillai ^a   Fong, Laura M ^a   Lauzon, Anne Marie ^a  

^a MCGILL UNIVERSITY   (Canada)

Author keywords

In vitro motility; Laser trap; Latch state; Phosphorylation; Velocity

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE MAGNESIUM; MYOSIN; ADENOSINE DIPHOSPHATE; ISOPROTEIN; MYOSIN HEAVY CHAIN;

ACTIN FILAMENT; ARTICLE; BINDING AFFINITY; CELL MOTILITY; DEPHOSPHORYLATION; IN VITRO STUDY; LATCH STATE; MUSCLE FUNCTION; OPTICAL TWEEZERS; PHASIC SMOOTH MUSCLE; PRIORITY JOURNAL; PROTEIN PURIFICATION; SMOOTH MUSCLE; TONIC SMOOTH MUSCLE; VELOCITY; WESTERN BLOTTING; ANIMAL; AVIAN STOMACH; BINDING SITE; BIOLOGICAL MODEL; CATTLE; CHICKEN; COMPARATIVE STUDY; ISOLATION AND PURIFICATION; LASER; METABOLISM; MICROFILAMENT; MICROSCOPY; MUSCLE CONTRACTION; PHOSPHORYLATION; PROTEIN BINDING; VASCULAR SMOOTH MUSCLE;

ADENOSINE DIPHOSPHATE; ANIMALS; BINDING SITES; BLOTTING, WESTERN; CATTLE; CHICKENS; GIZZARD; LASERS; MICROFILAMENTS; MICROSCOPY, VIDEO; MODELS, BIOLOGICAL; MUSCLE CONTRACTION; MUSCLE, SMOOTH; MUSCLE, SMOOTH, VASCULAR; MYOSIN HEAVY CHAINS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN ISOFORMS;

EID: 53449089110     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00100.2008     Document Type: Article

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