Proposed modifications to metabolic model for glycogen-accumulating organisms under anaerobic conditions

SummaryTreatment of human and dog oxalated plasma with 0.2 to 1.0 × 10−1 M 2.3-dithiopropanol (BAL) or dithiothreitol (DTT) at 2–4° C for 30 min results in the reduction of the vitamin-K dependent clotting factors II, VII, IX and X to the respective-SH derivatives. The reaction is pH dependent. Under aerobic conditions the delayed one stage prothrombin time can be partly reversed. Under anaerobic conditions a gradual prolongation of the one stage prothrombin time occurs without reversal.In very diluted plasma treated with the dithiols, prothrombin can be converted into thrombin if serum as source of active factors VII and X is added. In contrast SH factors VII, IX and X are inactive in the specific tests. Reoxidation to active factors II, VII, IX and X takes place during adsorption and elution of the SH derivatives. The experiments have indicated that not only factor II but also factors VII, IX and X have active-S-S-centres.

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METABOLISM OF 17α-HYDROXYPROGESTERONE-4-14C-17α-CAPROATE BY HOMOGENATES OF RAT LIVER AND HUMAN PLACENTA

Acta Endocrinologica ◽

10.1530/acta.0.0360511 ◽

1961 ◽

Vol 36 (4) ◽

pp. 511-519 ◽

Cited By ~ 6

Author(s):

Margaret Wiener ◽

Charles I. Lupa ◽

E. Jürgen Plotz

Keyword(s):

Rat Liver ◽

Human Placenta ◽

Steric Hindrance ◽

Placental Tissue ◽

Caproic Acid ◽

Major Product ◽

Side Chain ◽

Anaerobic Conditions ◽

Prolonged Action ◽

Long Acting

ABSTRACT 17α-hydroxyprogesterone-4-14C-17α-caproate (HPC), a long-acting progestational agent, was incubated with homogenates of rat liver and human placenta. The rat liver was found to reduce Ring A of HPC under anaerobic conditions to form allopregnane-3β,17α-diol-20-one-17α-caproate and pregnane-3β,17α-diol-20-one-17α-caproate, the allopregnane isomer being the major product. The caproic acid ester was neither removed nor altered during the incubation. Placental tissue did not attack HPC under conditions where the 20-ketone of progesterone was reduced. It is postulated that this absence of attack on the side chain is due to steric hindrance from the caproate ester, and that this may account for the prolonged action of HPC.

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Effect of Aerobic and Anaerobic Conditions on Chlorophenol Sorption in Wetland Soils

Soil Science Society of America Journal ◽

10.2136/sssaj2003.0787 ◽

2003 ◽

Vol 67 (3) ◽

pp. 787 ◽

Cited By ~ 13

Author(s):

Elisa D'Angelo ◽

K. R. Reddy

Keyword(s):

Wetland Soils ◽

Anaerobic Conditions ◽

Aerobic And Anaerobic ◽

Aerobic And Anaerobic Conditions

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Mechanistic Metabolic Model of Cancer Using DNA Dosages

SSRN Electronic Journal ◽

10.2139/ssrn.3335080 ◽

2019 ◽

Author(s):

Asoke Talukder ◽

Tapopriya Majumdar ◽

Rolf A. Heckemann

Keyword(s):

Metabolic Model

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Anaerobic treatment of soil wash fluids from a wood preserving site

Water Science & Technology ◽

10.2166/wst.1998.0278 ◽

1998 ◽

Vol 38 (7) ◽

pp. 63-72 ◽

Cited By ~ 3

Author(s):

K. M. Miller ◽

M. T. Suidan ◽

G. A. Sorial ◽

A. P. Khodadoust ◽

C. M. Acheson ◽

...

Keyword(s):

Soil Washing ◽

Anaerobic Treatment ◽

Integrated System ◽

Waste Stream ◽

Adsorptive Capacity ◽

Anaerobic Conditions ◽

Washing Process ◽

Polycyclic Aromatic ◽

Treatment Technologies ◽

Solvent Washing

An integrated system has been developed to remediate soils contaminated with pentachlorophenol (PCP) and polycyclic aromatic hydrocarbons (PAHs). This system involves the coupling of two treatment technologies, soil solvent washing and anaerobic biotreatment of the extract. Specifically, this study evaluated the effectiveness of the granular activated carbon (GAC) fluidized-bed reactor to treat a synthetic waste stream of PCP and four PAHs (naphthalene, acenaphthene, pyrene, and benzo(b)fluoranthene) under anaerobic conditions. This waste stream was intended to simulate the wash fluids from a soil washing process treating soils from a wood preserving site. The reactor achieved a removal efficiency of greater than 99.8% for PCP with conversion to its dechlorination intermediates ranging from 47% to 77%. Effluent, carbon extraction, and isotherm data also indicate that naphthalene and acenaphthene were removed from the liquid phase with efficiencies of 86% and 93%, respectively. Effluent levels of pyrene and benzo(b)fluoranthene were extremely low due to the adsorptive capacity of GAC for these compounds. Experimental evidence does not suggest that these compounds were chemically transformed within the reactor.

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Genome-Scale Metabolic Model as a Virtual Platform to Reveal the Environmental Contribution of Methanogens

Current Biotechnology ◽

10.2174/2211550105666160901125353 ◽

2017 ◽

Vol 6 (2) ◽

pp. 149-160 ◽

Cited By ~ 5

Author(s):

P. Chellapandi ◽

M. Bharathi ◽

R. Prathiviraj ◽

R. Sasikala ◽

M. Vikraman

Keyword(s):

Metabolic Model ◽

Environmental Contribution ◽

Virtual Platform ◽

Genome Scale

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Mechanism of inhibition of succinate oxidase by products of oxidation of o-dihydroxycoumarins

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19800641 ◽

1980 ◽

Vol 45 (2) ◽

pp. 641-652

Author(s):

Petr Zbořil

Keyword(s):

Inhibitory Activity ◽

Oxidase Activity ◽

Enzyme Preparation ◽

Inhibitory Effects ◽

Anaerobic Conditions ◽

Long Period ◽

Mechanism Of Inhibition ◽

Intermediary Product ◽

Succinate Oxidase ◽

By Products

Semiquinone is an intermediary product of the oxidation of daphnetin (7,8-dihydroxycoumarin) and esculetin (6,7-dihydroxycoumarin) by diphenol oxidase; its concentration rapidly decreases. When the oxidation is effected by ferricytochrome c, the concentration of the semiquinone remains practically constant for a long period. Similarly, the ability of the products of daphnetin oxidation by diphenol oxidase to inhibit succinate oxidase activity in mitochondrial fragments rapidly decreases with time; the decrease is considerably slower in the case of cytochrome c. The inhibitory activity of the product decreases with time also during esculetin oxidation by ferricyanide. This indicates that the inhibitory effects must be ascribed predominantly to the semiquinone, the quinone is less efficient. The inhibition of succinate oxidase or succinate dehydrogenase was strongly decreased when the enzyme preparation of Keilin and Hartree was incubated with esculetin and ferricyanide in the presence of KCN or under anaerobic conditions. This demonstrates that the reaction of the inhibitor with the enzyme either involves subsequent oxidations or that the inhibitor preferentially reacts with the oxidized form of the sensitive component of the respiratory chain. The second alternative is very little probable since there is no correlation between the degree of inhibition and the binding of the inhibitor to mitochondrial fragments.

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