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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)

Cardiac hypertrophy in the rabbit, secondary to pulmonary artery stenosis, results in a decrease in unloaded shortening velocity (Vmax) and maximum rate of isometric force development (dP/dtmax), while the peak isometric twitch tension is unchanged and time to peak tension (TPT) is increased. The principle hypothesis used to explain these results involve 1) slowing of myosin cross bridge movement as reflected in depressed myosin ATPase activity and 2) changes in excitation contraction coupling phenomena resulting in changes in intracellular Ca++ movement. Ca++ and actin activated myosin ATPase from the hypertrophied (H) muscles is depressed by 30%. Total initial heat, tension dependent heat and tension independent heat are depressed in H muscles by 57, 56, and 61% respectively. The rate of tension independent heat production in H preparations is depressed by 66%. From these data it is concluded that 61% of the depression in Vmax could be accounted for by the alteration in myosin with the reminder attributable to changes in EC coupling. Increased TPT can be accounted for by the change in rate of Ca++ flux as indicated by the alterated rate of tension independent heat evolution.
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PMID:The partitioning of altered mechanics in hypertrophied heart muscle between the sarcoplasmic reticulum and the contractile apparatus by means of myothermal measurements. 14 Jun 57

In the present investigation the results of a lead salt technique and two calcium salt techniques for the deomonstration of the activity of myosin adenosine triphosphatase in sections of both normal and pathological human skeletal muscle specimens are compared. It was seen that the histochemical results obtained by the different techniques are similar, especially with regard to the identification of fibre-types. It can be clearly stated, that the alkaline phosphatase activity present in muscle fibers of diseased skeletal msucles revealed only a very slight activity with the substrate ATP, so the alkaline phosphatase activity in general did not disturb the reliability of the different myosin ATPase techniques. Moreover it was found that the presence of the mitochondrial Ca2+ -ion activated ATPase with a high pH-optimum in muscle fibers did not give rise to faulty results. From studies with dinitrophenol it can be concluded that this substance activates the myosin ATPase present in type I fibres especially.
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PMID:The value of enzyme histochemical techniques in the classification of fibre types of human skeletal muscle. 2. The histochemical demonstration of myosin adenosine triphosphatase in skeletal muscles from adult patients with or with no diseases of the neuromuscular system. A comparison between results obtained by calcium salt and lead salt techniques. 14 Aug 52

CA2+-ATPase activity and light chains of myosin prepared from fast and slow muscles of rat guinea-pig and rabbit were studied during development from embryonic to old age to establish further correlation with the well-known developmental changes in contraction properties of these muscles. The changes involve the slow soleus muscle much more than the fast extensor digitorum longus muscle. Myosin-ATPase activity of the soleus muscle before or at birth is higher than in the muscle of adult animals. Myosin from the soleus muscle of embryos or newborn animals reveals light chains of myosin of both fast and slow type (with a preponderance of light chains of fast type in 26-days-old rabbit embryos). During postnatal development the amount of light chains of the fast type decreases, that of the slow type increases. Myosin from the soleus muscle of adult animals contains only light chains of the slow type. However, myosin from the soleus muscle of 30-months-old rats exhibits high myosin ATPase activity and contains light chains of myosin of both slow and fast type as in perinatal development. This is in agreement with the shortening of contraction time observed in this muscle in very old age. Thus developmental differentiation of myosine in the soleus muscle is followed by a trend of levelling out of the differences between fast and slow muscles of senescent animals. No such "biphasic" development is observed with respect to the fast extensor digitorum longus muscle.
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PMID:Differentiation of myosin in soleus and extensor digitorum longus muscle in differnt animal species during development. 14 53

The interaction of actin with myosin was studied in the presence of ATP at low ionic strength by means of measurements of the actin-activated ATPase activity of myosin and superprecipitation of actomyosin. At high ATP concentrations the ATPase activities of myosin, heavy meromyosin (HMM) and myosin subfragment 1 (S-1) were activated by actin in the same extent. At low ATP concentrations the myosin ATPase activity was activated about 30-fold by actin, whereas those of HMM and S-1 were stimulated only several-fold. This high actin activation of myosin ATPase was coupled with the occurrence of superprecipitation. The activation of HMM or S-1 ATPase by actin shows a simple hyperbolic dependence on actin concentration, but the myosin ATPase was maximally activated by actin at a 2:1 molar ratio of actin to myosin, and a further increase in the actin concentration had no effect on the activation. These results suggest the presence of a unit for actin-myosin interaction, composed of two actin monomers and one myosin molecule in the filaments.
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PMID:Presence of a unit for actin-myosin interaction during the superprecipitation of actomyosin. 14 84

A new, simple method for the isolation of actin from myxomycete plasmodia has been developed. Plasmodium myosin B was incubated at 55 degrees C for 15 min in the presence of ATP or was treated with 90% acetone. By this treatment myosin was denatured completely. Actin was then extracted with a dilute ATP and cysteine solution from the heat- or acetone-treated myosin B. The method is simple and almost pure actin was obtained in high yield. The purified G-actin polymerized to F-actin on addition of 0.1 M KCl or 2 mM MgCl2. The viscosity of the purified F-actin was 8-10 dl/g. The F-actin activated muscle myosin ATPase, and actomyosin synthesized from the F-actin and muscle myosin showed superprecipitation on addition of ATP.
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PMID:A simple method for the isolation of actin from myxomycete plasmodia. 14 66

Single muscle fibres were isolated by microdissection from freeze-dried samples of rabbit psoas and soleus muscles. The individual fibres were typed according to qualitative histochemical reactions for succinate dehydrogenase or NADH-tetrazolium reductase and for alkaline Ca2+-activated myofibrilla myosin ATPase after acid or alkaline preincubation. Methods are described for electrophoretic analysis by means of polyacrylamide disc electrophoresis in the presence of SDS of total myofibrilla proteins in single fibres after pre-extraction of soluble proteins. Fast-twitch white fibres revealed a myosin light chain pattern characteristic of "fast- type" myosin with three light chains of apparent molecular weights of 22,300 (LC1) 18,400 (LC2) and 16,000 (LC3). Fast-twitch red fibres were indistinguishable in this respect from fast-twist white fibres and showed an identical pattern of myosin light chains. Slow-twitch fibres could be characterized by a myosin light chain pattern typical of myosin of slow-twitch muscles with peptides of the apparent molecular weights of 23,500 (LC1Sa), 23,000 (LC1Sb) and 18,500 (LS2S). Slow-twitch fibres isolated from soleus as well as from psoas muscle were indistinguishable with regard to their myosin light chain patterns, thus suggesting that fibres of the same histochemical type correspond in their myosin light chain patterns irrespective of their origin from different muscles.
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PMID:Myosin light chain patterns of individual fast and slow-twitch fibres of rabbit muscles. 14 18

The moles of calcium bound by the left ventricle were 1.5 +/- 0.1, while those of the right ventricle were 2.9 +/- 0.2. The calcium binding constants were the same between myosins of the two cardiac ventricles. The Ca2+ binding constants were approximately 1.1 X 10(5) M-1 for both left and right ventricular myosins. Left ventricular myosin bound 1.3 +/- 0.1 mol of Mn2+, whereas right ventricular myosin bound 2.8 +/- 0.1 mol of Mn2+. The divalent cation Mn2+ only partially competed out Ca2+ (50%). Because of the partial competition, it seemed that Ca2+ and Mn2+ had some sights in common. These studies demonstrate a twofold difference in divalent cation binding (Ca2+, Mn2+) between left and right ventricular myosins. This variation in cation binding between the two ventricles is reflected in similar differences in myosin ATPase activity between the two ventricles.
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PMID:Binding of divalent cations by canine cardiac myosin: differences in normal right and left ventricles dependent upon number of light chains. 14 25

Human cardiac myosin isolated from operatively obtained samples of ventricular septum and left ventricular free wall of patients with asymmetric septal hypertrophy (ASH) was compared, with respect to structural and enzymatic properties, to myosin isolated from hearts of patients without heart disease. The following parameters were studied: 1) activation of myosin ATPase activity by K+-EDTA and Ca2+,2) molecular weight of the heavy and light chains of myosin as determined by electrophoretic migration in SDS-polyacrylamide gels, and 3) ability to form bipolar aggregates at low ionic strength, as examined by electron microscopy. No difference was present in any of these parameters between human cardiac myosin from patients with ASH and from patients without heart disease. Thus, the genetic defect present in patients with ASH is not expressed in the particular structural and functional characteristics of myosin evaluated in this study.
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PMID:Characterization of myosin from patients with asymmetric septal hypertrophy. 14 40

The Mg2+-dependent ATPase (adenosine 5'-triphosphatase) mechanism of myosin and subfragment 1 prepared from frog leg muscle was investigated by transient kinetic technique. The results show that in general terms the mechanism is similar to that of the rabbit skeletal-muscle myosin ATPase. During subfragment-1 ATPase activity at 0-5 degrees C pH 7.0 and I0.15, the predominant component of the steady-state intermediate is a subfragment-1-products complex (E.ADP.Pi). Binary subfragment-1-ATP (E.ATP) and subfragment-1-ADP (E.ADP) complexes are the other main components of the steady-state intermediate, the relative concentrations of the three components E.ATP, E.ADP.Pi and E.ADP being 5.5:92.5:2.0 respectively. The frog myosin ATPase mechanism is distinguished from that of the rabbit at 0-5 degrees C by the low steady-state concentrations of E.ATP and E.ADP relative to that of E.ADP.Pi and can be described by: E + ATP k' + 1 in equilibrium k' - 1 E.ATP k' + 2 in equilibrium k' - 2 E.ADP.Pi k' + 3 in equilibrium k' - 3 E.ADP + Pi k' + 4 in equilibrium k' - 4 E + ADP. In the above conditions successive forward rate constants have values: k' + 1, 1.1 X 10(5)M-1.S-1; k' + 2 greater than 5s-1; k' + 3, 0.011 s-1; k' + 4, 0.5 s-1; k'-1 is probably less than 0.006s-1. The observed second-order rate constants of the association of actin to subfragment 1 and of ATP-induced dissociation of the actin-subfragment-1 complex are 5.5 X 10(4) M-1.S-1 and 7.4 X 10(5) M-1.S-1 respectively at 2-5 degrees C and pH 7.0. The physiological implications of these results are discussed.
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PMID:Reaction mechanism of the magnesium ion-dependent adenosine triphosphatase of frog muscle myosin and subfragment 1. 14 77

F-actin monomer (F-monomer) is formed upon the addition of neutral salt to G-actin. Since F-monomer has a digestibility similar to that of F-actin and much lower than that of G-actin, it has been proposed that F-monomer has a conformation different from that of G-actin and similar to the conformation of the subunits in F-actin. To examine whether F-monomer will enhance the magnesium-activated myosin adenosine triphosphatase (Mg2+-ATPase) as much as F-actin, the ability of partially polymerized actin populations at equilibrium to activate the Mg2+-ATPase of heavy meromyosin was investigated. Correlations were made between ATPase activities and the polymerization state of actin as determined by measurements of viscosity and digestibility. No significant activation of the heavy meromyosin ATPase was observed under conditions where G-actin or mixtures of G-actin and F-monomer were present. As polymer formation occurred at higher actin concentrations, or with increased KCl concentrations, substantial activation characteristic of F-actin was observed. The data suggest that F-monomer may undergo a further conformational change as it forms nuclei or joins onto polymers. Alternatively, the site of actin which activates the myosin ATPase may involve the crevice between two adjacent actin subunits.
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PMID:Activation of heavy meromyosin adenosine triphosphatase by various states of actin. 15 Feb 86


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