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Query: EC:3.6.4.1 (myosin ATPase)
 1,140 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Muscle fibers are commonly classified histochemically into three types by the staining intensity for myosin ATPase combined with those for metabolic enzymes. Preincubation at pH 4.6 gives rise to three staining intensities of myosin ATPase which are also used for fiber typing. The two classification systems were compared by computer analysis of the individual staining profiles of over 2,500 fibers, and found not to be equivalent. The analysis showed metabolic heterogeneity among the fiber groups distinguished according to their differences in myosin ATPase.
Histochemistry 1979 Sep
PMID:Metabolic heterogeneity of muscle fibers classified by myosin ATPase. 4 Sep 25

While modification of six lysyl residues causes a near maximal decrease in Ca2+, K+, and actin + Mg2+ -activated myosin ATPase activities in rabbit skeletal muscle myosin, it takes nearly twice this number of modified lysyl groups to cause a similar alteration in canine cardiac myosin where trinitrophenylation is nonspecific. It appears that there are several rapidly reacting lysyl residues in cardiac myosin; the active site of cardiac myosin is protected by ATP after modification of a limited number of these rapidly reacting lysyl groups. In both myosins, after a charge modification of these rapidly reacting lysyl groups, 6 in rabbit skeletal muscle myosin and 10 in canine cardiac myosin, there is a decrease in Ca2+, K+, and actin + Mg2+ -stimulation of myosin but an activation of Mg2+ -stimulated myosin ATPase activity, thus making actin + Mg2+ -stimulated myosin ATPase activity more like activation with K+ or Ca2+ as compared to activation with Mg2+ alone.
Res Commun Chem Pathol Pharmacol 1979 Sep
PMID:Comparison of Mg2+ vs Ca2+, K+ and actin-activation of myosin after trinitrophenylation. 4 Dec 96

The interaction between paramyosin and myosin has been studied by enzymological methods. Clam adductor paramyosin inhibits the actin-activated, Mg2+-requiring ATPase of both clam adductor and rabbit skeletal muscle myosins. Myosin and paramyosin must be rapidly coprecipitated for this inhibition. Incubation with F-actin in the absence of ATP does not alter this effect. This inhibition follows a hyperbolic function with respect to paramyosin concentration. Slow precipitation by dialysis of myosin and paramyosin together leads to copolymers with actin-activated ATPase equivalent to that of slowly formed myosin filaments. Both kinds of slowly formed filaments have enzymatic properties distinct from those of the rapidly precipitated proteins. Paramyosin is competitive with F-actin for their effects upon myosin. The apparent affinity of myosin for F-actin is markedly reduced by association with paramyosin, but the extrapolated maximal velocity of actomyosin is unaffected. The specificity of this inhibition is strongly suggested by marked quantitative differences between native and cleaved paramyosins. No inhibition of intrinsic myosin ATPase by paramyosin is seen. These studies suggest that at least two types of condition-dependent association between myosin and paramyosin are possible. One class of interactions is associated with enzymic inhibition in rapidly coprecipitated filaments, whereas slowly formed cofilaments exhibit catalytic activity similar to that of identically treat-d myosin and have a characteristic 14.5 nm axial repeat.
Proc Natl Acad Sci U S A 1976 Sep
PMID:Myosin-paramyosin cofilaments: enzymatic interactions with F-actin. 13 57

Myosin was purified from the flight muscles of a flying (pigeon) and a nonflying (fowl) bird. Ki (ADP) of myosin ATPase of pigeon is higher, but the Km (ATP) is lower than that of fowl. The specific activity (mumole of Pi liberated/min/mg protein) is higher for the fowl. A0.5 (CaCl2) of myosin of both pigeon and fowl is similar. However, the two proteins differ in their interactions with ADP, ATP and p-chloromercuribenzoate. The two proteins have the same tyrosine, tryptophan and sulfhydryl contents. The electrophoretic patterns of the two myosins on SDS-polyacrylamide gels are different. These studies show significant molecular differences in the myosin derived from the flight muscles of a flying (pigeon) and a nonflying (fowl) bird.
Biochimie 1978 Sep 04
PMID:Comparative studies on myosin ATPase of a flying and nonflying bird. 15 58

Myosin was purified from rabbit alveolar macrophages in a form that could not be activated by actin. This myosin could be phosphorylated by an endogenous myosin light chain kinase, up to 2 mol of phosphate being incorporated/mol of myosin. The site phosphorylated was located on the 20,000-dalton myosin light chain. Phosphorylation of macrophage myosin was found to be necessary for actin activation of myosin ATPase activity. Moreover, the actin-activated ATPase activity was found to vary directly with the extent of myosin phosphorylation, maximal phosphorylation (2 mol of Pi/mol of myosin) resulting in an actin-activated MgATPase activity of approximately 200 nmol of Pi/mg of myosin/min at 37 degrees C. These results establish that phosphyoyration of the 20,000-dalton light chain of myosin is sufficient to regulate the actin-activated ATPase activity of macrophage myosin.
J Biol Chem 1979 Sep 25
PMID:Macrophage myosin. Regulation of actin-activated ATPase, activity by phosphorylation of the 20,000-dalton light chain. 15 17

Myosins purified from cardiac (porcine heart) and smooth (chicken gizzard) muscles were modified with 2,4,6-trinitrobenzenesulfonate (TNBS) and the effects on the kinetic properties of myosin ATPase [EC 3.6.1.3] were studied. The following results were obtained. 1. About 0.5 mol of TNBS per mol of myosin head was incorporated rapidly, irrespective of the presence of PP1 (2mM), into both types of myosin studied. 2. The size of the initial burst of P1 liberation for both myosins was found to be 0.5--0.6 mol/mol head. 3. The rapid incorporation of TNBS into cardiac muscle myosin was accompanied by a rapid decrease in the size of the initial P1 burst, and it was completely lost after modification for 20 min. However, smooth muscle myosin retained its P1 burst. 4. The EDTA (K+)-ATPase activity of both myosins modified in the presence or absence of PP1 decreased sharply with incorporation of TNBS. 5. Superprecipitation and ATPase activity of reconstituted actomyosin from cardiac myosin and skeletal F-actin decreased only after 10 min of modification with TNBS in the absence of PP1. 6. The spectra of TNP bound to myosins from cardiac and smooth muscles were unchanged by the addition of PP1. The above findings are compared with those previously obtained for skeletal muscle myosin [Miyanishi, T., Inoue, A., & Tonomura, Y. (1979) J. Biochem. 85, 747--753], and the structural and functional differences among the myosins derived from skeletal, cardiac, and smooth muscles are discussed.
J Biochem 1979 Sep
PMID:Modification of cardiac and smooth muscle myosins with 2,4,6-trinitrobenzenesulfonate. Evidence for differences in structure around the active sites of cardiac, smooth, and skeletal muscle myosin ATPase. 15 5

A plasma-membrane fraction was isolated from a post-nuclear extract of human neutrophils by centrifugation through a linear sucrose density gradient. This fraction exhibited a Ca2+-dependent adenosine triphosphatase (ATPase) activity that could be differentiated from mitochondrial or myosin ATPase and from plasma-membrane Mg2+-dependent ATPase. When assayed in the presence of [gamma-32P]ATP, the Ca2+-dependent ATPase reaction resulted in the formation of an acid-resistant hydroxylamine-sensitive bond between the gamma-[32P] phosphate group and a membrane protein subunit with an apparent mol.wt. of 135000. Half-maximal activating effect of Ca2+ was found at 82nM and 0.18 microM for the ATPase and the formation of the 32P-membrane complex respectively. Generation of the phosphorylated product attained the steady state at 0 degrees C by about 30s, and was rapidly reversed by ADP. These results suggest that the Ca2+-activated ATPase reaction occurs through the formation of a phosphoprotein intermediate, similar to that described for some Ca2+-dependent ATPase enzymes associated with Ca2+ transport. The possibility thus exists that the neutrophil Ca2+-dependent ATPase catalyses a process of Ca2+ extrusion from the cell, thereby participating in the regulation of several Ca2+-dependent neutrophil functions.
Biochem J 1979 Sep 15
PMID:Calcium ion-dependent adenosine triphosphatase activity and plasma-membrane phosphorylation in the human neutrophil. 16 Feb 22

Fibre-type classification of human skeletal muscle into type I and type II fibres is mostly based on their slight or strong staining with the myosin adenosine triphosphatase reaction. In order to evaluate the reliability of this screening technique a combined histochemical and biochemical study was performed on normal and diseased skeletal muscle of human subjects. In the present investigation activities of enzymes which play a role in the aerobic and anaerobic pathways and which can characterize fibre type, were examined in muscle specimens, with no apparent disease of the neuromuscular system. Special attention is given to the maximal activities of phosphofructokinase and fructose-1,6-diphosphatase, the rate limiting enzymes for the regulation of the glycolysis and glyconeogenesis, respectively. A most important feature of the biochemical findings is the constancy of the activity ratios of the examined enzymes. From these results and from the histochemical results it can be concluded that in apparently normal adult human skeletal muscle the ATP-ase technique for type I and type II typing is reliable. For fibres with an intermediate intensity of staining with the myosin ATPase technique of typing it is also necessary to apply other enzyme histochemical techniques.
Histochemistry 1976 Sep 13
PMID:The value of enzyme histochemical techniques in classifying fibre types of human skeletal muscle. 1. Adult skeletal muscles with no apparent disease of the neuromuscular system. 19 26

When studying enzymic and fluorescence properties of myosin and DTNB-treated myosin in the presence of K+, Na+, Li+, NH4+, Ca2+ and Mg2+ cations the following results were obtained. By the intrinsic protein fluorescence techniques no essential structural changes of myosin molecule at the dissociation of the DTNB light chain and activation myosin ATPase in the presence of different cations were found. The decrease of K+-EDTA-, the increase of Mg2+-activated and the stability of Ca2+-activated myosin ATPase may be the result of the modification of SH1 or SH2 sulfhydryl groups when treating the DTNB myosin in our conditions. The different level of decrease of the K+- and NH4+-activated myosin. ATPase may be explained by the fact, that myosin sulfhydryl groups have different effects on the activation of its ATPase by these cations.
Biokhimiia 1976 Sep
PMID:[Comparative study of myosin and DTNB-treated myosin with regard to ATP activity and fluorescence]. 97 74

We used the left ventricular (LV) end-systolic force-diameter (Fes-Des) relation to evaluate the effect of an alpha1-adrenoceptor antagonist (bunazosin hydrochloride) on the contractility of the beta-blocked left ventricle. Nine adult mongrel dogs were instrumented with ultrasonic crystals to measure LV diameter and a micromanometer to measure LV pressure. Beta-adrenergic and vagal blockade was induced with intravenous propranolol (2 mg/kg) and atropine (0.2 mg/kg), respectively, and preload was decreased by inferior vena caval occlusion. The slope (Ec) and extrapolated diameter intercept (Do) of the LV Fes-Des relation were derived from end-systolic data obtained in the control state (after beta-blockade) and after bunazosin infusion (1 mg/kg). Ec was used as a new index of LV contractility. After bunazosin infusion, the heart rate and Ec were decreased by 7 and 22%, respectively, in comparison with the control state, whereas Do did not change. These results indicate that alpha1-adrenoceptor blockade significantly reduces myocardial contractility in the beta-blocked canine heart, perhaps by decreasing the intracellular calcium concentration and/or myosin ATPase activity.
Jpn Circ J 1992 Sep
PMID:Effect of alpha 1-adrenoceptor blockade on the left ventricular force-length relationship in dogs. 135 97


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