The effects of environmental temperature on the properties of myofibrillar adenosine triphosphatase from various species of fish.
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ABSTRACT:
SUBMITTER: Johnston IA
PROVIDER: S-EPMC1177763 | biostudies-other | 1973 Aug
REPOSITORIES: biostudies-other
Similar Datasets
Project description:1. The steady-state kinetic behaviour of the ATPase (adenosine triphosphatase) of intact myofibrils was studied in the presence of both high and low concentrations of Ca2+ (0.25 mM and less than 10 nM respectively). 2. Kinetic data were collected over the initial linear phase of the assay, which lasts for 20--60s. To obtain consistent data we found it necessary to use either fresh myofibril preparations or preparations that had been stored in the presence of thiol compounds. 3. When assayed in the presence of 0.25 mM-Ca2+, the myofibrillar ATPase obeyed Michaelis-Menten kinetics over the range 0.03--5.0 mM-MgATP (Km 16 +/- 6 micrometer, V 0.4 +/- 0.1 mumol/min per mg). 4. At low Ca2+ concentrations (less than 10 nM) the myofibrillar ATPase displayed pronounced substrate inhibition, which was not observed at high Ca2+ concentrations. Thus increasing the MgATP concentration had the net effect of decreasing the ATPase activity at low Ca2+ relative to that at high Ca2+. This preferential effect of MgATP on the low-Ca2+ ATPase may be important in Ca2+ control. 5. The substrate inhibition that was observed at low Ca2+ was lost on storage or thiol modification of the myofibrils. 6. Under physiological conditions (2 mM-MgATP, I 0.15, pH 7.0), the ATPase of fresh and thiol-protected myofibrils displayed approx. 100-fold activation by Ca2+.
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Project description:Arrhenius plots of a membrane (Na+ + K+)-dependent ATPase (adenosine triphosphatase) activity showed characteristic discontinuities, whereas those of the associated K+-dependent phosphatase activity did not. These findings support the contention that the phosphatase activity does not depend on phospholipid in the same way as does the ATPase activity.
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Project description:The effects of oil droplet size and the formation of an interfacial protein film (IPF) on silver carp myofibrillar protein (MP)-oil composite gels were studied. MP- or Tween 80-stabilized camellia seed oil emulsions with different droplet sizes were prepared and added to MPs to prepare composite gels. The oil droplet size of the Tween 80-stabilized emulsion was significantly smaller (p < 0.05) than that of the MP-stabilized emulsion with the same homogenization speed. However, polymerization of Tween 80-stabilized emulsions during the preparation of the composite gels was found. Composite gels with the MP-stabilized emulsions of a small droplet size showed significantly improved water-holding capacity, texture, and dynamic rheological properties. Interfacial shear rheology studies revealed that the storage modulus (G') of the MP-stabilized emulsion composite gels was higher than that of the Tween 80-stabilized gels, and the tan δ of the MP-stabilized oil emulsion composite gels was smaller than that of the Tween 80-stabilized gels, indicating that stronger elastic gel structures were formed. These results suggested that the IPF formed in the MP-stabilized emulsion helped stabilize the oil droplets embedded in the protein gel network, and the smaller the droplet size, the more stable the composite gel. This work provides a better understanding of how oil emulsions interact with protein and affect the properties of MP-oil composite gels.
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Project description:This study investigated how Atlantic sturgeon cells respond to elevated temperatures, shedding light on the potential impacts of climate change on fish. Atlantic sturgeon (Acipenser oxyrinchus), an IUCN (International Union for Conservation of Nature) Red List species and evolutionarily related to paleonisiform species, may have considerable physiological adaptability, suggesting that this species may be able to cope with changing climatic conditions and higher temperatures. To test this hypothesis, the AOXlar7y cell line was examined at 20 °C (control) and at elevated temperatures of 25 °C and 28 °C. Parameters including proliferation, vitality, morphology, and gene expressions related to proliferation, stemness, and stress were evaluated. Additionally, to achieve a comprehensive understanding of cellular changes, mitochondrial and metabolic activities were assessed using Seahorse XF96. AOXlar7y cells adapted to 28 °C exhibited enhanced mitochondrial adaptability, plasticity, heightened cell proliferation, and increased hsp70 expression. Increased baseline respiration indicated elevated ATP demand, which is potentially linked to higher cell proliferation and heat stress defense. Cells at 28 °C also displayed elevated reserve respiration capacity, suggesting adaptation to energy demands. At 25 °C, AOXlar7y cells showed no changes in basal respiration or mitochondrial capacity, suggesting unchanged ATP demand compared to cells cultivated at 20 °C. Proliferation and glycolytic response to energy requirements were diminished, implying a connection between glycolysis inhibition and proliferation suppression. These research results indicate sturgeon cells are capable of withstanding and adapting to an 8 °C temperature increase. This cellular analysis lays a foundation for future studies aimed at a deeper understanding of fish cell physiological adaptations, which will contribute to a better knowledge of environmental threats facing Atlantic sturgeon and fish populations amid climate change.
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Project description:1. Homogenates of goldfish intestinal mucosa were separated into various fractions by differential centrifugation. Both adenosine-triphosphatase and beta-glycerophosphatase activities were found to be concentrated mainly in a membrane fraction which sedimented after 1200000g-min. 2. This membrane adenosine-triphosphatase system was activated by Na(+)+K(+) and inhibited by ouabain. 3. The ouabain-sensitive adenosine-triphosphatase activity was high and the ouabain-insensitive activity low in membrane fractions prepared from fish acclimatized previously to 8 degrees . The opposite was true for fish acclimatized to 30 degrees . 4. The Arrhenius plots of ouabain-sensitive and ouabain-insensitive adenosine-triphosphatase activities, measured from 5 degrees to 30 degrees , showed discontinuities at incubation temperatures that varied with the previous acclimatization temperature of the fish. 5. It is considered that modification of the membrane adenosine-triphosphatase system in goldfish intestinal mucosa may serve to regulate Na(+) transport at different environmental temperatures.
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Project description:Adult male fish were exposed to the various temperature acclimation conditions as outlined in the published manuscript and RNA was extracted from fish at each time point as listed in the experiment set description.
2005-11-03 | E-SMDB-2853 | biostudies-arrayexpress
Project description:1. An adenosine triphosphatase membrane system, dependent on Mg(2+) and activated further by Na(+)+K(+), was prepared from goldfish anterior intestine by differential centrifugation of homogenized intestinal scrapings. 2. The affinity of this preparation for Na(+) in the presence of K(+)+Mg(2+), for K(+) in the presence of Na(+)+Mg(2+) and for Mg(2+) alone, measured at 37 degrees , did not depend on the previous environmental temperature of the fish. When Na(+)+K(+) were added to preparations from 8 degrees -acclimatized fish the affinity for Mg(2+) increased; this was not seen with preparations from 30 degrees -acclimatized fish. 3. Part of the Mg(2+)-activated adenosine triphosphatase was inhibited by Na(+) and the amount of inhibition appeared to increase at high acclimatization temperatures. 4. This Na(+)-inhibited adenosine triphosphatase was separated from the (Na(+)+K(+))-activated enzyme by centrifugation on sucrose density gradients. 5. Preparations from 8 degrees -acclimatized fish contained less Mg(2+)-activated and more (Na(+)+K(+))-activated adenosine triphosphatase than did similar fractions from 30 degrees -acclimatized fish. 6. Acclimatization to different environmental temperatures might involve one form of adenosine triphosphatase changing to another. The origin of various membranes seen in microsomal fractions must, however, be established before this hypothesis can be tested further.
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Project description:1. The purification of an adenosine triphosphatase present in aqueous extracts of acetone-dried ox-heart mitochondria is described. 2. No evidence was found for the presence of more than one protein having adenosine-triphosphatase activity in these extracts. 3. The enzyme is less stable at 0 degrees than at 25 degrees but is stabilized by glycerol. 4. The activity is dependent on the presence of Mg(2+) or certain other bivalent metal cations. 5. The adenosine-triphosphatase activity of the Mg(2+)-activated enzyme is enhanced by 2,4-dinitrophenol. 6. The kinetics of Mg(2+) activation indicate that the ATP-Mg(2+) complex is the important substrate: free ATP and Mg(2+) are inhibitory. 7. This preparation of mitochondrial adenosine triphosphatase has many properties in common with the adenosine triphosphatase coupling factor from mitochondria (Racker, 1961).
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