Redox potential kinetics of the incubation medium during early development stages of Misgurnus fossilis loach

2017 ◽  
Vol 48 (1) ◽  
pp. 23-33
Author(s):  
A. B. Burlakov ◽  
V. I. Kuzmin ◽  
A. F. Gadzaov ◽  
D. L. Tytik ◽  
V. E. Kasatkin ◽  
...  
Keyword(s):  
Redox Potential ◽  
Early Development ◽  
Incubation Medium ◽  
Development Stages ◽  
Kinetics Of ◽  
Misgurnus Fossilis

scholarly journals Identification in skeletal muscle of a distinct extracellular pool of amino acids, and its role in protein synthesis

1971 ◽  
Vol 121 (5) ◽  
pp. 817-827 ◽  
Author(s):  
R. C. Hider ◽  
E. B. Fern ◽  
D. R. London
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Incubation Medium ◽  
Extensor Digitorum Longus ◽  
Extensor Digitorum ◽  
Longus Muscle ◽  
Kinetics Of

1. The kinetics of radioactive labelling of extra- and intra-cellular amino acid pools and protein of the extensor digitorum longus muscle were studied after incubations with radioactive amino acids in vitro. 2. The results indicated that an extracellular pool could be defined, the contents of which were different from those of the incubation medium. 3. It was concluded that amino acids from the extracellular pool, as defined in this study, were incorporated directly into protein.

Synthesis of nuclear and cytoplasmic proteins in the early development of fishes and echinoderms

Development ◽  
1971 ◽  
Vol 26 (3) ◽  
pp. 611-622
Author(s):  
Maya R. Krigsgaber ◽  
Alla A. Kostomarova ◽  
Tamara A. Terekhova ◽  
Tatiana A. Burakova
Keyword(s):  
Amino Acids ◽  
Early Development ◽  
Sea Urchin ◽  
Nuclear Volume ◽  
Sea Urchin Embryos ◽  
Cytoplasmic Proteins ◽  
Specific Activities ◽  
Strongylocentrotus Nudus ◽  
Silver Grains ◽  
Misgurnus Fossilis

Synthesis of nuclear and cytoplasmic proteins was studied biochemically and autoradiographically in early loach (Misgurnus fossilis) and sea-urchin (Strongylocentrotus nudus) embryos. After incubation with [14C]amino acids for 5–120 min the ratio of the specific activities of nuclear, mitochondrial and 12000 g supernatant proteins was shown to be equal approximately to 6:1:2 in loach embryos and to 8:4:3 in sea-urchin embryos independently of the duration of labelling. After incubation with [3H]amino acids the number of silver grains per unit section was on the average 2·4 times higher for nuclei than it was for cytoplasm at mid-blastula and mid-gastrula stages. At the mid-gastrula the vegeto-animal gradient of protein synthesis was found. A higher level of the synthesis of nuclear proteins as compared with that of cytoplasmic proteins appears to be related to an increase in the nuclear volume and the nucleo-cytoplasmic ratio during the early development of the loach and sea-urchin embryos.

scholarly journals Biochemical Engineering Parameters for Hydrometallurgical Processes: Steps towards a Deeper Understanding

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
K. Kundu ◽  
A. Kumar
Keyword(s):  
Redox Potential ◽  
Metal Ion ◽  
Good Control ◽  
Point Of View ◽  
Rate Equations ◽  
Biochemical Engineering ◽  
Mining Operations ◽  
Feasible Option ◽  
Engineering Parameters ◽  
Kinetics Of

Increasing interest in biomining process and the demand for better performance of the process has led to a new insight toward the mining technologies. From an engineering point of view, the complex network of biochemical reactions encompassed in biomining would best be performed in reactors which allow a good control of the significant variables, resulting in a better performance. The subprocesses are in equilibrium when the rate of particular metal ion; for example, iron turnover between the mineral and the bacteria, is balanced. The primary focus is directed towards improved bioprocess kinetics of the first two subprocesses of chemical reaction of the metal ion with the mineral and later bacterial oxidation. These subprocesses are linked by the redox potential and controlled by maintenance of an adequate solids suspension, dilution rate, and uniform mixing which are optimised in bioreactors during mining operations. Rate equations based on redox potential such as ferric/ferrous-iron ratio have been used to describe the kinetics of these subprocesses. This paper reviews the basis of process design for biomining process with emphasis on engineering parameters. It is concluded that the better understanding of these engineering parameters will make biomining processes more robust and further help in establishing it as a promising and economically feasible option over other hydrometallurgical processes worldwide.

scholarly journals Vegetated Habitats Trophically Support Early Development Stages of a Marine Migrant Fish in a Coastal Lagoon

2020 ◽  
Vol 43 (2) ◽  
pp. 424-437
Author(s):  
Cristina Andolina ◽  
Piero Franzoi ◽  
Andrew Lloyd Jackson ◽  
Antonio Mazzola ◽  
Salvatrice Vizzini
Keyword(s):  
Early Development ◽  
Coastal Lagoon ◽  
Development Stages

scholarly journals Kinetics of Reduction of Fe(III) Complexes by Outer Membrane Cytochromes MtrC and OmcA of Shewanella oneidensis MR-1

2008 ◽  
Vol 74 (21) ◽  
pp. 6746-6755 ◽  
Author(s):  
Zheming Wang ◽  
Chongxuan Liu ◽  
Xuelin Wang ◽  
Matthew J. Marshall ◽  
John M. Zachara ◽  
...  
Keyword(s):  
Redox Potential ◽  
Outer Membrane ◽  
Kinetic Data ◽  
Shewanella Oneidensis ◽  
Reorganization Energy ◽  
Second Order ◽  
Metal Species ◽  
Stopped Flow ◽  
Kinetics Of ◽  
Kinetics Of Reduction

ABSTRACT Because of their cell surface locations, the outer membrane c-type cytochromes MtrC and OmcA of Shewanella oneidensis MR-1 have been suggested to be the terminal reductases for a range of redox-reactive metals that form poorly soluble solids or that do not readily cross the outer membrane. In this work, we determined the kinetics of reduction of a series of Fe(III) complexes with citrate, nitrilotriacetic acid (NTA), and EDTA by MtrC and OmcA using a stopped-flow technique in combination with theoretical computation methods. Stopped-flow kinetic data showed that the reaction proceeded in two stages, a fast stage that was completed in less than 1 s, followed by a second, relatively slower stage. For a given complex, electron transfer by MtrC was faster than that by OmcA. For a given cytochrome, the reaction was completed in the order Fe-EDTA > Fe-NTA > Fe-citrate. The kinetic data could be modeled by two parallel second-order bimolecular redox reactions with second-order rate constants ranging from 0.872 μM−1 s−1 for the reaction between MtrC and the Fe-EDTA complex to 0.012 μM−1 s−1 for the reaction between OmcA and Fe-citrate. The biphasic reaction kinetics was attributed to redox potential differences among the heme groups or redox site heterogeneity within the cytochromes. The results of redox potential and reorganization energy calculations showed that the reaction rate was influenced mostly by the relatively large reorganization energy. The results demonstrate that ligand complexation plays an important role in microbial dissimilatory reduction and mineral transformation of iron, as well as other redox-sensitive metal species in nature.

Kinetics of N-substituted phenothiazines and N-substituted phenoxazines oxidation catalyzed by fungal laccases

2009 ◽  
Vol 4 (1) ◽  
pp. 62-67 ◽  
Author(s):  
Lidija Tetianec ◽  
Juozas Kulys
Keyword(s):  
Electron Transfer ◽  
Redox Potential ◽  
Reorganization Energy ◽  
Outer Sphere ◽  
Initial Reaction Rate ◽  
Initial Reaction ◽  
Type I ◽  
Electron Transfer Mechanism ◽  
Recombinant Laccase ◽  
Kinetics Of

AbstractLaccase-catalyzed oxidation of N-substituted phenothiazines and N-substituted phenoxazines was investigated at pH 5.5 and 25°C. The recombinant laccase from Polyporus pinsitus (rPpL) and the laccase from Myceliophthora thermophila (rMtL) were used. The dependence of initial reaction rate on substrate concentration was analyzed by applying the laccase action scheme in which the laccase native intermediate (NI) reacts with a substrate forming reduced enzyme. The reduced laccase produces peroxide intermediate (PI) which in turn decays to the NI. The calculated constant (kox) values of the PI formation are (6.1±3.1)×105 M−1s−1 for rPpL and (2.5±0.9)×104 M−1s−1 for rMtL. The bimolecular constants of the reaction of the native intermediate with electron donor (kred) vary in the interval from 2.2×105 to 2.1×107 M−1s−1 for rPpL and from 1.3×102 to 1.8×105 M-1s−1 for rMtL. The larger reactivity of rPpL in comparison to rMtL is associated with the higher redox potential of type I Cu of rPpL. The variation of kred values for both laccases correlates with the change of the redox potential of substrates. Following outer sphere (Marcus) electron transfer mechanism the calculated activationless electron transfer rate and the apparent reorganization energy are 5.0×107 M−1s−1 and 0.29 eV, respectively.

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