Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Myosin has been purified from the following cultured cell lines: normal rat kidney fibroblast (NRK), HeLa-Rhino (HeLa), human choriocarcinoma, human acute lymphoblastic leukemia, rat hepatoma (HTC), monkey kidney (VERO), pigmented mouse melanoma, Y-1 rat adrenal cortex, and growth hormone-secreting GH-1. Myosin constitutes 0.5-5.4% of the protein of these cells. It was not detected in washed human erythrocytes or in two types of mouse plasmacytoma cells. Two methods for the purification of myosin from cultured cells have been employed. With Method I highly purified myosin was prepared by Sepharose 4B and DEAE-cellulose chromatography from 10(10) L-929 cells as well as from mouse uterus. Those myosins have similar molecular and subunit weights as well as ATPase activity but are immunologically distinct. Method II involving ultracentrifugation and Sepharose 4B chromatography, is suitable for the production of moderately pure myosin in good yield from as few as 5-10(7) cells (five 100-mm Petrie dishes).
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PMID:The purification and quantitation of myosin from cultured cells. 13 88

A method for isolation of a soluble ATPase from rat liver mitochondria after freeze thaw cycling is described. Two enzymatically active fractions were separated by DEAE-cellulose chromatography (ATPase 1 and ATPase 2). ATPase 1 has been purified 300 fold. ATPase 1 was homogenous as judged by polyacrylamide gel electrophoresis. The optimum pH of the enzyme was 5.8-6.0 and the optimum temperature was 45 degrees C. The enzyme follows Michaelis-Menten kinetics: Km (9 X 10(-4) M), Vmax (23,6 mumoles Pi released X min -1 X mg protein -1). The enzyme hydrolysed nucleoside triphosphates, but was inactive upon nucleoside di and monophosphates, glucose 6-phosphate, phosphoserine, pyrophosphate and glycerol 2-phosphate. In contrast to membrane bound ATPase, cations have no effect on the enzyme activity. Nucleoside di and mono phosphates and glycerol 2 phosphate inhibited competitively the enzyme. The enzyme was not affected by oligomycin, but was stimulated by lactate, 2-mercaptoethanol and dithiothreitol.
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PMID:Studies of soluble rat liver mitochondrial acid ATPases. I. Purification and catalytic properties of ATPase 1. 13 98

Myosin was isolated from the smooth muscles of small intestine of calf with good yield and its properties were compared with the myosin's properties from the skeletal rabbit muscle. The crude myosin was purified by means of DEAE-cellulose column chromatography, using a KCl gradient. The purity of the preparations was checked spectrophotometrically by the densities of adsorption D280/D260, viscosimmetrically by the sensitivity to ATP, electrophoretically and by ultracentrifugation. By the above-mentioned properties the smooth muscle myosin was similar to the high-purified skeletal muscle myosin. A comparative study of the enzymatic properties of myosin from two types of tissues, showed the following differences: (1) in the dependence the Ca2+-ATPase activity on the KCl concentration in the incubation medium; (2) in the degree of myosin activation by actin in the presence of Mg2+; (3) in the behaviour of Ca2+-ATPase dependence on pH; (4) the different temperature optima of the ATPase activity.
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PMID:[Preparation and the properties of a highly purified preparation of myosin from smooth muscles]. 13 28

A DNA-dependent ATPase formed after T4 phage infection is purified to apparent homogeneity. The molecular weight of the purified enzyme is 50 000 when determined by glycerol gradient centrifugation and by sodium dodecylsulfate/polyacrylamide gel electrophoresis. The enzyme at an earlier stage in purification (prior to DEAE-cellulose chromatography) exists as a complex with a molecular weight of 100000. However, molecular weight determinations by Sephadex gel chromatography give considerably decreased molecular weights for the complex and for the enzyme after DEAE-cellulose chromatography. The enzyme is stimulated to varying degrees by a variety of single-stranded polydeoxyribonucleotides or by single-stranded DNA, but no chemical change in the polynucleotide has been detected as a result of the enzyme action.
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PMID:Purification and properties of a DNA-dependent ATPase induced by bacteriophage T4. 14 Aug 3

1. Beef-heart mitochondrial ATPase (F1) is inactivated and dissociated by incubation with 0.85 M LiCl. ATP partly protects against inactivation. Three dissociation products could be identified after chromatography on diethylaminoethylcellulose: the delta subunit which is not adsorbed, the beta subunit which may be eluted from the column, and the alpha and gamma subunits which remain bound to the column. 2. Aurovertin binds to dissociated F1 with a fluorescence enhancement equal to about 30% that found with F1. Unlike intact F1 which shows two kinetically separated phases of fluorescence enhancement, only a fast phase is found with dissociated enzyme. 3. Fluorescence measurements at varying aurovertin and protein concentrations indicate that aurovertin binds to dissociated F1 in a simple 3-component reaction with dissociation constant 0.4 muM. There are two indistinguishable binding sites, calculated on the basis of the initial F1 concentration before dissociation. 4. The beta subunit was isolated from dissociated F1 by DEAE-cellulose chromatography. It has no ATPase activity but reacts with aurovertin with a fluorescence enhancement similar to that of dissociated F1. 5. The isolated beta subunit contains one aurovertin binding site with a dissociation constant of 0.56 muM. 6. It is concluded that F1 contains two beta subunits.
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PMID:The binding of aurovertin to isolated beta subunit of F1 (mitochondrial ATPase). Stoicheiometry of beta subunit in F1. 14 45

The preparation of highly purified F1-ATPase from Micrococcus sp. ATCC 398 by application of DEAE-Sepharose CL-6B chromatography as final step is described. This enzyme consists of five subunits of different molecular weight: alpha (65000), beta (55000),gamma (35000), delta (20000), and epsilon (17000). Disc electrophoresis on 5% polyacrylamide gels removes the epsilon-polypeptide yielding an active ATPase complex with four different subunits: alpha, beta, gamma, delta. Additionally, by variation of the ionic strength delta can (partly) removed allowing the isolation by disc electrophoresis of an active ATPase complex which consists only of three different subunits alpha, beta, and gamma. If the DEAE-Sepharose chromatography is carried out in the absence of diisopropyl phosphofluoridate (auto)proteolysis yields both an active ATPase with the subunits alpha+ (mol. wt 61000), beta, gamma, and delta and an inactive protein complex with the subunits alpha+, beta, gamma, delta, and two additional polypeptides a (mol. wt 38000) and b (mol. wt 23000). The latter two polypeptides are supposedly fragments of alpha+-chains which have become partially cleaved by (auto)proteolysis.
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PMID:F1-ATPase from Micrococcus sp. ATCC 398. Purification by ion-exchange chromatography and further characterization. (Auto)proteolysis and dissociative effects. 14 65

An isolation procedure is worked out and properties are studied of CF1 ATPase from chloroplasts with changed submolecular structure. The enzyme, isolated by chlorophorm treatment, produced Ca-dependent ATPase activity in water solution. As compared with the enzyme isolated by well known Lien and Racker method, the enzyme preparation obtained is slightly activated by heating, is not activated by trypsin and has a lesser ability to recover ATP synthesis in EDTA-treated chloroplasts. Purification on DEAE-Sephadex produced the enzyme preparation free of delta-subunit. Chlorophorm treatment is suggested to change submolecular protein structure, in particular, loosening of the link of delta-subunit with other enzyme subunits. The data obtained suggest that delta-subunit participates in the binding of CF1 ATPase with chloroplast membrane.
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PMID:[Isolation and properties of CF1 ATPase chloroplasts with changed submolecular structure]. 14 26

ATPase (ATP phosphohydrolase, EC 3.6.1.3) activity was shown in the soluble fraction of rat liver micochondria. Two molecular forms (ATPase 1 and 2) were isolated. ATPase 1 has already been studied. The present paper deals with the purification method of ATPase 2 which was achieved by the following steps: (NH4)2SO4 precipitation. DEAE-cellulose chromatography, hydroxyapatite chromatography, Sephadex G100 filtration and AMP-Sepharose affinity chromatography. The purified protein was characterized by bidimensional polyacrylamide gel electrophoresis. Molecular weight evaluated by SDS-polyacrylamide gel electrophoresis and Sephadex G100 gel filtration was found to be 61 500 +/- 3000.
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PMID:Purification of a soluble ATPase from rat liver mitochondria by AMP-Sepharose affinity chromatography. 15 Aug 61

An inhibitory protein for Mg2+-activated actomyosin ATPase from rabbit skeletal muscle was prepared from frozen chicken gizzard and purified by DEAE-Sephadex chromatography and gel filtration. 2. The inhibition by this protein was released by the addition of skeletal muscle troponin C and was independent of gizzard tropomyosin. 3. Localization of the inhibitory protein in gizzard muscle tissue and gizzard thin filaments was demonstrated by immunohistological techniques and immunodiffusion tests.
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PMID:Isolation and localization from chicken gizzard of an inhibitory protein for Mg2+-activated skeletal muscle actomyosin ATPase. 15 12

A protein was isolated from a human erythrocyte lysate with an apparent molecular weight of 23,000--24,000 daltons. This protein was purified by batch DEAE cellulose followed by column DEAE cellulose chromatography and a gradient of NaCl. On sodium dodecyl sulfate acrylamide electrophoresis, the erythrocyte protein comigrated with muscle troponin inhibitor. An isoelectric precipitation (pH 9.25) was used for the separation of muscle troponin inhibitor from a complex with another troponin component. Both the erythrocyte protein and the muscle troponin inhibitor partially inhibited muscle myosin Ca2+ and K+-EDTA ATPase activity. Furthermore, they inhibited actin-activated Mg2+-ATPase of muscle myosin. The inhibitory effects were absent in the presence of muscle troponin calcium-binding component. Muscle troponin inhibitor and the erythrocyte troponin inhibitor-like protein bound to muscle myosin when myosin was precipitated twice at low ionic strength. The presence of a troponin inhibitor-like protein in erythrocytes suggests that it may be a component in the regulation of contractile activity.
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PMID:Erythrocyte troponin inhibitor-like protein: isolation and characterization. 15 37


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