Photosensitization of Mitochondrial Adenosine-Triphosphatase and Adenylate Kinase by Hematoporphyrin Derivative in Vitro

1985 ◽  
pp. 161-167 ◽  
Author(s):  
Nai-Wu Fu ◽  
Shu-Yong Yeh ◽  
Chin Chang ◽  
Xiu-Hua Zhao ◽  
Li-Sung Chang
Keyword(s):  
Adenylate Kinase ◽  
Adenosine Triphosphatase ◽  
Hematoporphyrin Derivative

In Vitro Effect of Chlorquine and Picroliv on Plasmodium Berghei Induced Alterations in the Activity of Adenosine Triphosphatase, Aryl Hyrocarbon Hydroxylase Enzymes and Malondialdehyde in spleen Explant Culture

2020 ◽  
Vol 20 ◽  
Author(s):  
Anchal Trivedi ◽  
Aparna Misra ◽  
Esha Sarkar ◽  
Anil K. Balapure
Keyword(s):  
Drug Resistance ◽  
Plasmodium Berghei ◽  
Adenosine Triphosphatase ◽  
Explant Culture ◽  
Need To Evaluate ◽  
Mda Content ◽  
High Level ◽  
Vitro Effect ◽  
Positive Effect

Background: In recent years, great progress has been made in reducing the high level of malaria suffering worldwide. There is a great need to evaluate drug resistance reversers and consider new medicines against malaria. There are many approaches to the development of antimalarial drugs. Specific concerns must be taken in to account in these approaches, in particular there requirement for very in expensive and simple use of new therapies and the need to limit drug discovery expenses. Important ongoing efforts are the optimisation of treatment with available medications, including the use of combination therapy. The production of analogs of known agents and the identification of natural products, the use of compounds originally developed against other diseases, the assessment of overcoming drug resistance and the consideration of new therapeutic targets. Liver and spleen are the important organs which are directly associated with malarial complications. Aim: An analysis the Activity of Adenosine Triphosphatase, Aryl Hyrocarbon Hydroxylase Enzymes and Malondialdehyde in spleen Explant Culture. Objective: To determine in-Vitro Effect of Chlorquine and Picroliv on Plasmodium Berghei Induced Alterations in the Activity of Adenosine Triphosphatase, Aryl Hyrocarbon Hydroxylase Enzymes and Malondialdehyde in spleen Explant Culture. Material and method: 1-Histological preparation of spleen explants for paraplast embedding 2-Biochemicalstudies (Enzymes (Atpase, ALP&GST) and the level of protein, Malondialdehyde (MDA). Result: Splenomegalyis one of the three main diagnostic parameters of malaria infection besides fever and anaemia. Many enzymes present in the liver and spleen may also be altered or liberated under different pathological conditions. Enzymes (ATPase, ALP&GST) and the level of protein, Malondialdehyde (MDA) content was found to increase in the liver and spleen explants during malarial infection. In the liver and spleen derived from parasitized CQ treated animals, the activity of all the above enzymes (ATPase, ALP&GST) and the level of protein & MDA of liver/spleen reversed towards the normal for all the 4or3 days of incubations. Picroliv efficacy decreased with the increment of parasitaemia and at 60%parasitaemia. Conclusion: Alkalinephosphatase (ALP) was found to increase with increasing parasitaemia. After the addition of Picroliv to the medium, a decrement in the activity was observed up to day 4 of culture.A similar positive effect of Picroliv was observed on the ATPase and ALP activity of spleen explants.DNA and protein contents also increased in the parasitized liver cultured in the presence of picroliv.On the contrary, in the spleen explants DNA, protein and MDA content were found to decrease after Picroliv supplementation to the culture medium.

scholarly journals A mutation affecting a second component of the F0 portion of the magnesium ion-stimulated adenosine triphosphatase of Escherichia coli K12. The uncC424 allele

1977 ◽  
Vol 164 (1) ◽  
pp. 193-198 ◽  
Author(s):  
F Gibson ◽  
G B Cox ◽  
J A Downie ◽  
J Radik
Keyword(s):  
Escherichia Coli ◽  
Electron Transport ◽  
Fluorescence Quenching ◽  
Mutant Strain ◽  
Mutant Allele ◽  
Adenosine Triphosphatase ◽  
Magnesium Ion ◽  
New Mutation ◽  
Similar Phenotype

A new mutant strain of Escherichia coli in which phosphorylation is uncoupled from electron transport was isolated. The new mutant strain has a similar phenotype to the uncB mutant described previously; results from reconstitution experiments in vitro indicate that the new mutation also affects a component of the F0 portion of the Mg2+-stimulated adenosine triphosphatase. A method was developed to incorporate mutant unc alleles into plasmids. Partial diploid strains were prepared in which the uncB402 allele was incorporated into the plasmid and the new unc mutation into the chromosome, or vice versa. Complementation between the mutant unc alleles was indicated by growth on succinate, growth yields on glucose, ATP-dependent transhydrogenase activities, ATP-induced atebrin-fluorescence quenching and oxidative-phosphorylation measurements. The gene in which the new mutation occurs is therefore distinct from the uncB gene, and the mutant allele was designated uncC424.

scholarly journals Studies in vitro on the effects of 1H,2H,4H(5H)-octafluorocyclohexane and 1H,4H(2H)-nonafluorocyclohexane on enzymes and organelles

1969 ◽  
Vol 114 (4) ◽  
pp. 785-792 ◽  
Author(s):  
Jayasree Nath ◽  
H G Bray
Keyword(s):  
Adenosine Triphosphatase ◽  
Marked Decrease ◽  
Reductase Activity ◽  
Electron Microscopic Examination ◽  
Electron Microscopic ◽  
Toxic Compound ◽  
Marked Inhibition ◽  
Liver Homogenates ◽  
Nadh Cytochrome

A comparison has been made of the effect of 1H,2H,4H(5H)-octafluorocyclohexane, which is highly toxic (LD50 17mg./kg. in rats), and of 1H,4H(2H)-nonafluorocyclohexane, which is relatively non-toxic (LD50>440mg./kg. in rats), on the respiration of rat liver homogenates and mitochondria in vitro. 1H,2H,4H(5H)-Octafluorocyclohexane strongly inhibited the respiration of both homogenates and mitochondria, but neither compound had any significant effect on glycolysis or on glutamate dehydrogenase or NADH–cytochrome c reductase activity. 1H,2H,4H(5H)-Octafluorocyclohexane, however, caused a very marked inhibition of cytochrome oxidase activity, causing an almost complete lesion in this region of the respiratory chain. 1H,4H(2H)-Nonafluorocyclohexane was without effect in this respect. A marked decrease in turbidity of mitochondrial suspensions at 520nm. was caused by addition of both compounds, the effect being greater with 1H,2H,4H(5H)-octafluorocyclohexane. ATP, Mg2+ and bovine serum albumin did not reverse these changes. Mitochondrial adenosine triphosphatase activity was increased twofold by the toxic compound, but only slightly by the non-toxic compound. Electron-microscopic examination of mitochondria treated with 1H,2H,4H(5H)-octafluorocyclohexane revealed gross morphological damage, whereas the effect of 1H,4H(2H)-nonafluorocyclohexane appeared to be merely to cause swelling. The results obtained account, to some extent at any rate, for the toxic effects of 1H,2H,4H(5H)-octafluorocyclohexane.

Uptake and Retention of Hematoporphyrin Derivative in an in Vivo/in Vitro Model of Cerebral Glioma

Neurosurgery ◽  
1985 ◽  
Vol 17 (6) ◽  
pp. 883-890 ◽  
Author(s):  
Andrew H. Kaye ◽  
George Morstyn ◽  
Robert G. Ashcroft
Keyword(s):  
In Vitro Model ◽  
Hematoporphyrin Derivative ◽  
Cerebral Glioma ◽  
Vitro Model

scholarly journals The lipopolysaccharide transporter complex LptB2FG also displays adenylate kinase activity in vitro dependent on binding partners LptC/LptA

2021 ◽  
pp. 101313
Author(s):  
Tiago Baeta ◽  
Karine Giandoreggio-Barranco ◽  
Isabel Ayala ◽  
Elisabete C.C. M. Moura ◽  
Paola Sperandeo ◽  
...  
Keyword(s):  
Adenylate Kinase ◽  
Kinase Activity ◽  
Binding Partners

The nature of the fibril

1950 ◽  
Vol 137 (886) ◽  
pp. 70-71
Keyword(s):  
Adenosine Triphosphatase ◽  
Fibrin Clot ◽  
High Ionic Strength ◽  
Contractile Element ◽  
Rich Medium ◽  
Experimental Proof ◽  
Essential Components ◽  
Muscle Biochemistry ◽  
Water Holding

One of the chief problems in muscle biochemistry at the present time is to elucidate the way in which the component proteins of the muscle fibril are assembled to give a contractile element. The myosin-actin-ATP system is so unusual that it is generally thought to contain the essential components for contraction, but it is true to say that in vitro studies of this system are merely suggestive, and have generally led to speculations on the mechanism of contraction which are either dubious or not amenable to experimental proof. The first difficulty is that in the molecular sense the nature of the interaction of myosin and actin is not clear. Under the conditions of salt concentration at which actin and myosin separately are dispersed in solution, the effect of ATP on actomyosin is to produce a large decrease in viscosity. This has been interpreted as a dissolution of the links which bind actin and myosin together, liberating the component molecules from an anastomosed network of fibres. More specifically, it seems due to the competition of ATP for certain groupings which not only link up with actin, but are responsible for the adenosine-triphosphatase activity of myosin. In salt-poor medium, where myosin by itself is no longer soluble, the effect of ATP is to produce an intense synaeresis, which superficially is suggestive of ‘contraction’. There is no reason to suppose that the action of ATP in this case is at all different from that in a salt-rich medium ; the breaking of the actin-myosin links is followed, however, by a further interaction which is reminiscent of the synaeresis of a fibrin clot. Jordan & Oster (1948) have concluded from light-scattering studies that, even at high ionic strength, ATP causes not a dissociation of actin and myosin, but an increased coiling of the actomyosin particle. There is no doubt, however, that the mechanical properties of actomyosin fibres in the presence of ATP are more in keeping with the original explanation that linkages responsible for anastomosis are broken down. What bearing the synaeresis phenomenon has upon the mechanism of contraction is not very clear, since the changes involved are inter- and not intramolecular. It is possible that the interaction reflects the means by which these water-holding proteins are tightly packed in the fibril.

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