Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0009443 (cold)
 92,137 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Oligomycin-insensitive ATPase (ATP phosphohydrolase, EC 3.6.1.3) was purified from brown adipose tissue mitochondria. It had a specific activity of 50 units/mg which could be increased up to 85 units/mg by KHCO3. The isolated enzyme represented less than 0.5% of the initial membrane proteins.2. The enzyme had a molecular weight equal to beef heart ATPase and was composed of five subunits with molecular weights of 56 200, 54 300, 33 500, 13 400 and 9500 respectively. 3. Isolated ATPase was labile while cold and was activated by the divalent cations Mn2+, Mg2+, Co2+ and Cd2+. The optimum ATP/Mg2+ ratio found was 1.58 and the enzyme had a maximum activity at pH 8.5; the Km was 220 micrometer. 4. The ATPase activity was 55% inhibited by aurovertin. The isolated enzyme enhanced the fluorescence of aurovertin, quenched by ATP and Mg2+ and enhanced by ADP. 5. Oligomycin sensitivity and cold stability of isolated ATPase was restored by its reconstitution with both brown adipose tissue and beef heart particles depleted of ATPase. 6. The results presented demonstrate that the low ATPase activity of brown adipose tissue mitochondria is due to a reduced content of ATPase.
 ...
PMID:Purification and properties of mitochondrial adenosine triphosphatase of hamster brown adipose tissue. 14 14

A partially purified soluble ATPase (ATP phosphohydrolase, EC 3.6.1.3) from pea cotyledon mitochondria was characterized. Inhibition patterns with azide, NaF, and cold, and a stimulation by 2,4-dinitrophenol were typical of F1-ATPases from mammalian mitochondria. The enzyme hydrolysed GTP, ITP, and ATP, but not CTP, UTP, ADP, or IDP. ATPase and ITPase activities were strongly inhibited by ADP and to a lesser extent by IDP. Distinctive properties of the pea mitochondrial enzyme were activation by high concentrations of CaCl2 and stimulation by NaCl.
 ...
PMID:Partial characterization of a soluble ATPase from pea cotyledon mitochondria. 14 76

The extranuclear mitochondrial oligomycin-resistant mutation of Aspergillus nidulans, (oliA1), was transferred asexually into four nuclear oligomycin-resistant strains of different phenotypes. In all four cases, the possession of the nuclear plus extranuclear mutation led to an increase in the in vivo level of oligomycin resistance. In two cases, the altered cytochrome spectrum and impaired growth ability determined by (oliA1) were suppressed by the nuclear mutations. In the third case, the in vitro oligomycin resistance of the double mutant ATPase was dramatically increased above that of either of the component single mutant strains, indicating a synergystic interaction between the nuclear and extranuclear gene products. In the fourth case, the double mutant became cold-sensitive. A new extranuclear mitochondrial oligomycin-resistant mutation (oliB332) is described. This mutant is phenotypically similar to, though not identical with, (oliA1) but is separable by recombination. A range of nuclear oligomycin-resistant mutants have been mapped. Despite presenting five distinctly different phenotypes, they all map at the same locus.
 ...
PMID:Nuclear-extranuclear interactions affecting oligomycin resistance in Aspergillus nidulans. 14 64

1. Preincubation of MgATP submitochondrial particles with EDTA or Tris.HCl liberated a measurable amount of ATPase inhibitor that could be rapidly purified using only trichloroacetic acid precipitation and heat treatment. 2. In spite of the emergence of high ATPase activity, a considerable amount of ATPase inhibitor was left in the particles. Comparative analysis of other submitochondrial preparations indicated that only AS-particles were effectively depleted. 3. The high ATPase activity of inhibitor-deficient particles, was labile at low temperature provided that the exposure to cold was done in the presence of MgATP. Other nucleotides could not substitute for ATP. Glycerol inhibited and salts enhanced the cold inactivation of membrane-bound F1-ATPase. Isolation of F1-ATPase from cold-inactivated particles yielded a soluble preparation of correspondingly lower activity. 4. It is concluded that together with the increase of ATPase activity, the ATP-dependent cold lability of membrane-bound F1-ATPase and the dislocation of ATPase inhibitor at non operative sites reveal the extent of ATPase complex disorganization.
 ...
PMID:Cold lability of membrane-bound F1-ATPase. 14 42

Previous studies on fish Mg2+Ca2+ activated myofibrillar ATPases have been extended to species inhabiting diverse thermal environments. Cold adapted ATPases have considerably higher catalytic centred activities at low temperatures than warm adapted ATPases. Differences in cell temperature have also lead to evolutionary modifications in thermodynamic activation parameters. The free energies (deltaG2+), enthalpies (deltaH2+) and entropies (deltaS2+) of activation of the Mg2+Ca2+ myofibrillar ATPase are positively correlated with adaptation temperature. Myofibrils with CaATP-2 as substrate in the absence of Mg2+ will hydrolyse ATP by a mechanism not associated with fibril shortening. Differences in activation enthalpies (deltaHH) between cold and warm adapted Ca2+-activated myofibrillar ATPases are less pronounced than for the physiological ATPase. Furthermore the Ca2+-activated ATPase showed no relationship between environmental temperature and substrate turnover number or free energy of activation (deltaG2+).
 ...
PMID:Further studies on the adaptation of fish myofibrillar ATPases to different cell temperatures. 14 87

Rh-pos. human red cells sensitized with IgG-Anti-D showed at 4 degrees C an intracellular Na+-accumulation, which was amplified by an increase in the Na+-concentration in the incubation medium. This increase of the intracellular Na+-concentration may be due to a passive Na+-influx since the Na+-K+-ATPase system does not work at this temperature. At the optimal reaction-temperature of the enzyme the Na+-K+-ATPase activity of the sensitized Rh-pos. red cells was inhibited proportionally to the anti-D concentration. Both the amplified Na+-influx and the inhibition of the active Na+-transport caused an osmotic hemolysis. The hemoglobin release was significant above the anti-D titer step of 1:512. This mechanism suggests that the intravasular part of the immunohemolysis with Rh incompatibility was generated by an impaired active and passive cation transport following the antigen-antibody reaction. This suggestion is supported by the fact that IgG-Anti-D neither stimulated the complement system nor the intravascular monocyte mediated cell lysis, since the activity of the effector cells is reduced by the surplus of sensitized red cells and the presence of other inhibiting IgG immunoglobulins. The biochemical relationship of the Rh-D-antigen and the Na+-K+ATPase both located on membrane lipoproteins, may be the reason why only the antigen-antibody reaction in the Rh-D system impaired the cation transport. The antigen-antibody reaction of IgM-Anti-A and of the cold agglutinin IgM-Anti-I reacting with glycolipid and with glycoprotein membrane antigens respectively did not impair the cation transport after complement inactivation.
 ...
PMID:[Impairment of the cation transport on Rh-pos. human red cells after incubation with IgG-anti-D (author's transl)]. 14 46

The effects of different salts and concentrations of ethylene diamine tetraacetic acid (EDTA) on the histochemically demonstrable myofibrillar ATPase reaction have been investigated. Serial frozen sections from the vastus lateralis muscle of rats, rabbits and guinea pigs were treated with cold (4 degrees) dipotassium EDTA solution and then incubated for myofibrillar ATPase activity. The results showed that all type I muscle fibres exhibited enhanced ATPase activity while type II fibres demonstrated either very low, moderate or intense reaction suggesting the existence of three different sub-populations. None of these effects was observed if the sections were immersed in magnesium chloride solution after preincubation in cold diK+ EDTA. Preincubation in cold non-ionic EDTA, disodium or tetrasodium EDTA did not affect the regular ATPase reaction pattern, while preincubation in warm (19 degrees--21 degrees C) solutions of the same salts resulted in reversal of the regular pattern of ATPase activity. The present histochemical data emphasise the importance of K+, Mg++ and temperature during preincubation of muscle fibres in EDTA before the demonstration of myofibrillar ATPase activity. Moreover, preincubation in a cold solution of diK+ EDTA may be valuable in the histochemical detection of distinct sub-populations of type II muscle fibres and certainly distinguished between type II white and type II red.
 ...
PMID:The effect of EDTA on the histochemical myofibrillar ATPase reaction. 15 88

1. F1-ATPase has been extracted by the diphosphatidylglycerol procedure from mitochondrial ATPase complexes that differ in ATPase activity, cold stability, ATPase inhibitor and magnesium content. 2. The ATPase activity of the isolated enzymes was dependent upon the activity of the original particles. In this respect, F1-ATPase extracted from submitochondrial particles prepared in ammonia (pH 9.2) and filtered through Sephadex G-50 was comparable to the enzyme purified by conventional procedures (Horstman, L.L. and Racker, E. (1970) J. Biol. Chem. 245, 1336--1344), whereas F1-ATPase extracted from submitochondrial particles prepared in the presence of magnesium and ATP at neutral pH was similar to factor A (Andreoli, T.E., Lam, K.W. and Sanadi, D.R. (1965) J. Biol. Chem. 240, 2644--2653). 3. No systematic relationship has been found in these F1-ATPase preparations between their ATPase inhibitor content and ATPase activity. Rather, a relationship has been observed between this activity and the efficiency of the ATPase inhibitor-F1-ATPase association within the membrane. 4. It is concluded that the ATPase activity of isolated F1-ATPase reflects the properties of original ATPase complex provided a rapid and not denaturing procedure of isolation is employed.
 ...
PMID:F1-ATPase from different submitochondrial particles. 15 27

In the present study, the question of whether the two myosin active sites are identical with respect to ATP binding and hydrolysis was reinvestigated. The stoichiometry of ATP binding to myosin, heavy meromyosin, and subfragment-1 was determined by measuring the fluorescence enhancement caused by the binding of MgATP. The amount of irreversible ATP binding and the magnitude of the initial ATP hydrolysis (initial Pi burst) was determined by measuring [gamma-32P]ATP hydrolysis with and without a cold ATP chase in a three-syringe quenched flow apparatus. The results show that, under a wide variety of experimental conditions: 1) the stoichiometry of ATP binding ranges from 0.8 to 1 mol of ATP/myosin active site for myosin, heavy meromyosin, and subfragment-1, 2) 80 to 100% of this ATP binding is irreversible, 3) 70 to 90% of the irreversibly bound ATP is hydrolyzed in the initial Pi burst, 4) the first order rate constant for the rate-limiting step in ATP hydrolysis by heavy meromyosin is equal to the steady state heavy meromyosin ATPase rate only if the latter is calculated on the basis of two active sites per heavy meromyosin molecule. It is concluded that the two active sites of myosin are identical with respect to ATP binding and hydrolysis.
 ...
PMID:The mechanism of the skeletal muscle myosin ATPase. I. Identity of the myosin active sites. 15 64

Storage of red cells for three weeks at 4 C under blood bank conditions resulted in a rise in intracellular Na+ and a fall in intracellular K+ with concomitant opposite changes in Na+ and K+ levels in the suspending plasma. A decline in red blood cell ATP during the storage period did not appear to be contributing to the changes. Increasing red blood cell ATP to levels 2 to 3 times normal did not prevent the cation changes from occurring. When assayed at 37 C in the presence of added Mg++, ouabain-sensitive membrane ATPase activity and kinetics of activation by Na+ were unaffected by the three week period of cold storage. However, when assayed at 4 C without added Mg++, simulating the conditions of storage, ATPase activity was negligible. Sodium and potassium did not change when red blood cells with normal ATP content were stored at 20 to 24 C even in the absence of added Mg++. Thus, a major cause for the development of cation changes in the red blood cell during blood bank storage in the temperature which inhibits membrane ATPase, allowing cations to leak unopposed into and out of the red blood cells.
 ...
PMID:Sodium and potassium changes in blood bank stored human erythrocytes. 15 33


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>