Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

TN-C was purified from bovine cardiac muscle. In the absence of Ca-2+, cardiac TN-C has an intrinsic sedimentation coefficient of 1.93 S and a molecular weight of 18 000 daltons. Cardiac TN-C reverses the inhibitory effect of skeletal TN-I on the Mg-2+-activated ATPase of a skeletal synthetic actomyosin preparation in the presence of skeletal tropomyoson. Circular dichroism (CD) studies indicate that cardiac TN-C undergoes a major conformational change upon binding Ca-2+. A similar response is elicited by Sr-2+, whereas Mg-2+ has a much less pronounced effect. The presence of Mg-2+ does not alter the net effects of either Ca-2+ or Sr-2+. Cardiac TN-C is rich in acidic amino acid residues. UV absorption, near UV CD, and fluorimetric studies show that the protein lacks tryptophan and has a relatively high phenylalanine to tyrosine ratio. The results of this study invite direct comparisons with results reported for the skeletal muscle analogue of cardiac TN-C.
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PMID:Molecular and biological studies on cardiac muscle calcium-binding protein (TN-C). 12 76

When stoichiometric amounts of tropomyosin (TM) are bound to F-actin in the presence of 2 mM ATP, the MG2+-activated acto-heavy meromyosin (HMM) ATPase is inhibited by about 60% in 5 mM MgCl2-30 mM KCl. If the concentration of MgCl2 is reduced to 1 mM, the inhibition disappears because TM no longer binds to F-actin. Increasing the concentration of KCl to 100 mM restores both the binding and the inhibition. Thus, the binding of TM alone to F-actin causes significant inhibition of the ATPase provided that the HMM is saturated with ATP. (When the HMM is not saturated, TM activates the ATPase). When TM alone can bind stoichiometrically to F-actin, addition of troponin I (TN-I) increases the inhibition from 60% to about 85%, but the TM binding to F-actin is not affected. Under conditions such that TM alone neither inhibits the acto-HMM ATPase nor binds to F-actin, the inhibition caused by TN-I plus TM still approaches 100%. Direct binding studies under these conditions show that TN-I induces binding between TM and F-actin. A dual role for TN-I is proposed: first, TN-I can induce TM to bind to F-actin, causing inhibition of the ATPase; and second, TN-I can itself enhance the inhibition of the ATPase in a cooperative manner. The addition of TN-C in the absence of CA2+ has only a limited effect on the first role, but seems to be able to block completely the cooperative inhibition caused by TN-I such that the residual inhibition is a function only of the TM which remains bound.
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PMID:Correlation between the inhibition of the acto-heavy meromyosin ATPase and the binding of tropomyosin to F-actin: effects of Mg2+, KCl, troponin I, and troponin C. 12

The three major components of bovine cardiac troponin were separated by successive chromatography on sulfopropyl-Sephadex and DEAE-Sephadex columns in the presence of 6 M urea. All three of the bovine cardiac troponin subunits were necessary to restore full troponin activity in both skeletal and cardiac actomyosin ATPase assay systems. The 38,000-dalton subunit bound tropomyosin, and the 20,000-dalton subunit bound calcium, like skeletal TN-T and TN-C, respectively. The 28,000 component, although presumably analogous to skeletal TN-I, gave very little inhibition of actomyosin ATPase activity. Differences between cardiac and skeletal troponin subunits were also found in the elution patterns from ion exchange columns and in amino acid composition, thus demonstrating a significant muscle-type specificity.
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PMID:Separation and characterization of the troponin components from bovine cardiac muscle. 12 74

The enzymic activity of Mg2+- or Ca2+-stimulated ATPase from Escherichia coli was inhibited by one of the troponin components, TN-I, and by mitochondrial ATPase inhibitor (F1-inhibitor). The inhibitory ability of component TN-I against Mg2+-stimulated AtPase activity was lost after digestion of component TN-I with trypsin. The Mg2+-stimulated ATPase activity inhibited by component TN-I was completely restored by the addition of another troponin component TN-C.
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PMID:Inhibition of E coli ATPase activity by a troponin component, TN-I, and by mitochondrial ATPase inhibitor. 16 Mar 25

By indirect immunofluorescence microscopy, the reactivities of extra- and intrafusal muscle fibers with antibodies against troponin (TN) components were studied in an avian slow muscle, the anterior latissimus dorsi (ALD) of the chicken. Serial cross sections of the muscle were exposed to antibodies specific to TN components (TN-T, -I, and -C) from adult chicken breast and ventricular muscles. In extrafusal fibers, four distinct categories were identified on the basis of differential reactivity with these antibodies. The predominant population of fibers (greater than 95%) reacted weakly only with antiventricular TN-C. The second type of fibers (less than 5%) was stained with antibodies raised against breast TN components. The third group of fibers (less than 1%) was labeled not only with antibreast TN components, but also with antiventricular TN-T and -C. The last class of fibers (less than 1%) reacted with antibodies directed against ventricular TN-T and -C. These results were correlated with myofibrillar ATPase staining patterns of fibers. In intrafusal muscle fibers of this muscle, the same four types of fibers were observed; in these fibers, however, there appeared to be a longitudinal variation in the reactivity. In conclusion, the slow ALD muscle of the adult chicken contains populations of both extrafusal and intrafusal fibers which are heterogeneous in reactivity with TN component antibodies.
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PMID:Distribution of polymorphic forms of troponin components in extra- and intrafusal fibers of an avian slow muscle. 623 17

1. Alterations in troponin subunits in myocardial infarction were studied in the dog heart by the analysis of troponin-tropomyosin complex, i.e, native tropomyoin, of total structural proteins in SDS gel electrophoresis, and by the measurement of degree of activation of actomyosin-ATPase by Ca++. 2. At 12 to 24 hours after coronary ligation, reductions in TN-C and tropomyosin were observed followed by a decrease in TN-I at 48 hours. The relative contents of these subunits were the lowest at 72 hours to 7 days falling to less than 10% of those in the non-ischemic myocardium. On the contrary, TN-T was preserved through the course of myocardial infarction. 3. Actomyosin-ATPase activity was increased at 12 to 24 hours after coronary ligation and then reduced rapidly at 24 to 48 hours together with the degradation of myosin. However, the activation of actomyosin-ATPase by Ca++-troponin-tropomyosin was reduced already at 12 hours simultaneously with the reduction in TN-C, and almost completely lost at 48 hours. 4. Troponin subunits and actomyosin-ATPase activity returned to those of the control myocardium at 28 days after coronary ligation indicating the recovery of infarcted tissue.
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PMID:Alterations in cardiac troponin subunits in myocardial infarction. 645 21