Role of MgATP and inorganic phosphate ions in cross-bridge kinetics in insect (Lethocerus colossicus) flight muscle. 1990

B L Marcussen, and M Kawai
Department of Anatomy, College of Medicine, University of Iowa, Iowa City 52242.

The cross-bridge cycle and related kinetic parameters in insect muscles is determined in a skinned fiber system. Small preparations consisting of 2 fibers each are isolated from indirect flight muscles from a giant water bug, Lethocerus Colossicus, and used for experiments. These preparations have stretch activation with the rate constant parameters becoming stable at 5% above the slack length and longer. The preparations are activated in the presence of (mM:) 6 CaEGTA (pCa 4.5), 1 Mg++, 10 NaN3, 10 MOPS (pH 7.00), 15 creatine phosphate, 350 unit/ml kinase, 0.05-5mM MgATP, 0-16mM phosphate, and the ionic strength adjusted to 140mM with K proprionate. The kinetic parameters are assessed by small amplitude (0.25%) length oscillations at varying frequencies (0.25-350Hz), and by following amplitude and phase shift in tension. From these, the complex modulus is determined by the ratio of the stress to the strain in the frequency domain. Exponential processes (B) and (C) are identified in the complex modulus data; process (A) is very small or absent. Process (B) is known as oscillatory work, and is equivalent to delayed tension in step analysis. Process (C) is equivalent to phase 2 of the same. When the MgATP concentration is increased, the rate constants of both processes (B) and (C) increase and saturate. With increasing concentrations of phosphate, the rate constant of processes (B) also increases. The MgATP and phosphate dependence of the rate constants are analyzed in terms of a cross-bridge scheme with 5 states, and the following kinetic parameters are deduced: K1 = 0.7mM-1, k2 = 900s-1, k-2 = 180s-1, K2 = 5, and k3 = 70s-1.(ABSTRACT TRUNCATED AT 250 WORDS)

UI MeSH Term Description Entries
D007313 Insecta Members of the phylum ARTHROPODA composed or organisms characterized by division into three parts: head, thorax, and abdomen. They are the dominant group of animals on earth with several hundred thousand different kinds. Three orders, HEMIPTERA; DIPTERA; and SIPHONAPTERA; are of medical interest in that they cause disease in humans and animals. (From Borror et al., An Introduction to the Study of Insects, 4th ed, p1). Insects,Insect
D007537 Isometric Contraction Muscular contractions characterized by increase in tension without change in length. Contraction, Isometric,Contractions, Isometric,Isometric Contractions
D009119 Muscle Contraction A process leading to shortening and/or development of tension in muscle tissue. Muscle contraction occurs by a sliding filament mechanism whereby actin filaments slide inward among the myosin filaments. Inotropism,Muscular Contraction,Contraction, Muscle,Contraction, Muscular,Contractions, Muscle,Contractions, Muscular,Inotropisms,Muscle Contractions,Muscular Contractions
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D010710 Phosphates Inorganic salts of phosphoric acid. Inorganic Phosphate,Phosphates, Inorganic,Inorganic Phosphates,Orthophosphate,Phosphate,Phosphate, Inorganic
D005426 Flight, Animal The use of wings or wing-like appendages to remain aloft and move through the air. Animal Flight,Animal Flights,Flights, Animal
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D017301 Ca(2+) Mg(2+)-ATPase An enzyme that catalyzes the hydrolysis of ATP and is activated by millimolar concentrations of either Ca(2+) or Mg(2+). Unlike CA(2+)-TRANSPORTING ATPASE it does not require the second divalent cation for its activity, and is not sensitive to orthovanadate. (Prog Biophys Mol Biol 1988;52(1):1). A subgroup of EC 3.6.1.3. ATPase, Calcium Magnesium,ATPase, Magnesium,Adenosinetriphosphatase, Calcium, Magnesium,Adenosinetriphosphatase, Magnesium,Calcium Magnesium ATPase,Calcium Magnesium Adenosinetriphosphatase,Magnesium ATPase,Magnesium Adenosinetriphosphatase,Adenosine Triphosphatase, Calcium, Magnesium,Adenosine Triphosphatase, Magnesium,Ca Mg-ATPase,Ca2+-Mg2+ ATPase,Calcium Magnesium Adenosine Triphosphatase,Mg2+-ATPase,Mg2+-Dependent ATPase,ATPase, Ca2+-Mg2+,ATPase, Mg2+-Dependent,Adenosinetriphosphatase, Calcium Magnesium,Ca Mg ATPase,Ca2+ Mg2+ ATPase,Magnesium Adenosine Triphosphatase,Mg2+ ATPase,Mg2+ Dependent ATPase
D066298 In Vitro Techniques Methods to study reactions or processes taking place in an artificial environment outside the living organism. In Vitro Test,In Vitro Testing,In Vitro Tests,In Vitro as Topic,In Vitro,In Vitro Technique,In Vitro Testings,Technique, In Vitro,Techniques, In Vitro,Test, In Vitro,Testing, In Vitro,Testings, In Vitro,Tests, In Vitro,Vitro Testing, In

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