scholarly journals The relationship between redox enzyme activity and electrochemical potential—cellular and mechanistic implications from protein film electrochemistry

2011 ◽  
Vol 13 (17) ◽  
pp. 7720 ◽  
Author(s):  
Andrew J. Gates ◽  
Gemma L. Kemp ◽  
Chun Yip To ◽  
James Mann ◽  
Sophie J. Marritt ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Electrochemical Potential ◽  
Redox Enzyme ◽  
Protein Film ◽  
The Relationship

Influence of Enzyme Activity of Bacteria and Leucocytes in Raw Milk on Age Gelation after UHT Processing

1984 ◽  
Vol 47 (2) ◽  
pp. 105-107 ◽  
Author(s):  
BARBARA P. KEOGH ◽  
G. PETTINGILL
Keyword(s):  
Enzyme Activity ◽  
High Temperature ◽  
Inhibitory Action ◽  
Raw Milk ◽  
Bacterial Counts ◽  
High Temperature Processing ◽  
The Relationship ◽  
Ultra High Temperature

An investigation was undertaken into the relationship between the enzyme activity of cells harvested from raw milk and time taken for age gelation (TAG) to occur in the milk after ultra-high-temperature processing. It was shown that there was no relationship between the TAG and the bacterial counts on milk agar at 30°C or 7°C nor was there a relationship between the counts and the level of enzyme activity of the harvested cells. There was, however, a significant correlation between the level of enzyme activity of the harvested cells and the TAG. When extra bovine leucocytes were added to raw milk before processing, the TAG was increased. This suggested that there was an inhibitory action of leucocytes in development of age gelation.

The Relationship of the −5, −8, and −24 Variant Alleles in African Americans to Triosephosphate Isomerase (TPI) Enzyme Activity and to TPI Deficiency

Blood ◽  
1998 ◽  
Vol 92 (8) ◽  
pp. 2959-2962 ◽  
Author(s):  
Arthur Schneider ◽  
Linda Forman ◽  
Beryl Westwood ◽  
Catherine Yim ◽  
James Lin ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
African American ◽  
African Americans ◽  
Triosephosphate Isomerase ◽  
Small Subset ◽  
Nucleotide Substitutions ◽  
Severe Deficiency ◽  
American Society ◽  
Relationship Of ◽  
The Relationship

Abstract In 424 African-American and 75 white subjects, we found that the −5 (TPI 592 A→G), −8 (TPI 589 G→A), and −24 (TPI 573 T→G) variants in the triosephosphate isomerase (TPI) gene occurred frequently (41.0%) in the African-American subjects but did not occur in the whites. These data suggest that this set of polymorphisms may turn out to be one of the higher-incidence molecular markers of African lineage, a surprising finding because others had reported that these nucleotide substitutions were restricted to a small subset of African Americans who had been characterized as TPI-deficiency heterozygotes. Additionally, we investigated the relationship of these variants to TPI-enzyme activity. Although the variant substitutions (occurring in three haplotypes: −5 alone, −5 −8, and −5 −8 −24) were associated with moderate reduction in enzyme activity, severe-deficiency heterozygotes could not be identified with certainty, and none of the haplotypes were restricted to subjects with marked reduction of enzyme activity. Three subjects were homozygous for the −5 −8 haplotype, a finding inconsistent with the putative role of this haplotype as the cause of a null variant incompatible with life in homozygotes. Despite these findings, the possibility remains that the −5 −8 or −5 −8 −24 haplotypes may in some instances contribute to compound heterozygosity and clinical TPI deficiency. © 1998 by The American Society of Hematology.

Change Analysis of Enzyme Activity under Different Conditions of Film Remnant in Soil

2012 ◽  
Vol 518-523 ◽  
pp. 39-43
Author(s):  
Xiao Guang Zhao ◽  
Yuan Yuan Guan ◽  
Wen Yu Huang
Keyword(s):  
Enzyme Activity ◽  
Enzyme Activities ◽  
Scientific Basis ◽  
Soil Enzyme ◽  
Soil Microorganism ◽  
Soil Enzyme Activities ◽  
Change Analysis ◽  
Soil Material ◽  
The Relationship

In this paper, simulated experiments were performed in pots by using soil materials in different conditions of film remnant. Based on the research on soil microorganism quantity trends of soil enzyme activities were analyzed systematically: soil without film remnant, soil with film remnant for 5, 10, 15 and 20 years. By analyzing crop progress, the relationship with soil material was studied, in order to provide scientific basis for the variation laws between different conditions of film remnant and the activity of soil enzyme.

Inter-tissue differences in mitochondrial enzyme activity, RNA and DNA in rainbow trout (Oncorhynchus mykiss)

1998 ◽  
Vol 201 (24) ◽  
pp. 3377-3384 ◽  
Author(s):  
S. C. Leary ◽  
B. J. Battersby ◽  
C. D. Moyes
Keyword(s):  
Enzyme Activity ◽  
Rainbow Trout ◽  
Oncorhynchus Mykiss ◽  
Citrate Synthase ◽  
Mitochondrial Protein ◽  
Molecular Organization ◽  
Mitochondrial Rna ◽  
Mitochondrial Enzyme ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
The Relationship

We examined whether the relationships between mitochondrial enzyme activity, mitochondrial DNA (mtDNA) and mitochondrial RNA (mtRNA) were conserved in rainbow trout (Oncorhynchus mykiss) tissues that differ widely in their metabolic and molecular organization. The activity of citrate synthase (CS), expressed either per gram of tissue or per milligram of total DNA, indicated that these tissues (blood, brain, kidney, liver,cardiac, red and white muscles) varied more than 100-fold in mitochondrial content. Several-fold differences in the levels of CS mRNA per milligram of DNA and CS activity per CS mRNA were also observed, suggesting that fundamental differences exist in the regulation of CS levels across tissues. Although tissues varied 14-fold in RNA g-1, poly(A+) RNA (mRNA)was approximately 2 % of total RNA in all tissues. DNA g-1 also varied 14-fold across tissues, but RNA:DNA ratios varied only 2.5-fold. The relationship between two mitochondrial mRNA species (COX I, ATPase VI) and one mitochondrial rRNA (16S) species was constant across tissues. The ratio of mtRNA to mtDNA was also preserved across most tissues; red and white muscle had 10- to 20-fold lower levels of mtDNA g-1 but 7- to 10-fold higher mtRNA:mtDNA ratios, respectively. Collectively, these data suggest that the relationship between mitochondrial parameters is highly conserved across most tissues, but that skeletal muscles differ in a number of important aspects of respiratory gene expression ('respiratory genes'include genes located on mtDNA and genes located in the nucleus that encode mitochondrial protein) and mtDNA transcriptional regulation.

Voltammetric characterization of the aerobic energy-dissipating nitrate reductase of Paracoccus pantotrophus: exploring the activity of a redox-balancing enzyme as a function of electrochemical potential

2007 ◽  
Vol 409 (1) ◽  
pp. 159-168 ◽  
Author(s):  
Andrew J. Gates ◽  
David J. Richardson ◽  
Julea N. Butt
Keyword(s):  
Nitrate Reductase ◽  
Nitrate Reduction ◽  
Reductase Activity ◽  
Electrochemical Potential ◽  
Intact Cells ◽  
Protein Film ◽  
Protein Film Voltammetry ◽  
Voltammetric Studies ◽  
Paracoccus Pantotrophus

Paracoccus pantotrophus expresses two nitrate reductases associated with respiratory electron transport, termed NapABC and NarGHI. Both enzymes derive electrons from ubiquinol to reduce nitrate to nitrite. However, while NarGHI harnesses the energy of the quinol/nitrate couple to generate a transmembrane proton gradient, NapABC dissipates the energy associated with these reducing equivalents. In the present paper we explore the nitrate reductase activity of purified NapAB as a function of electrochemical potential, substrate concentration and pH using protein film voltammetry. Nitrate reduction by NapAB is shown to occur at potentials below approx. 0.1 V at pH 7. These are lower potentials than required for NarGH nitrate reduction. The potentials required for Nap nitrate reduction are also likely to require ubiquinol/ubiquinone ratios higher than are needed to activate the H+-pumping oxidases expressed during aerobic growth where Nap levels are maximal. Thus the operational potentials of P. pantotrophus NapAB are consistent with a productive role in redox balancing. A Michaelis constant (KM) of approx. 45 μM was determined for NapAB nitrate reduction at pH 7. This is in line with studies on intact cells where nitrate reduction by Nap was described by a Monod constant (KS) of less than 15 μM. The voltammetric studies also disclosed maximal NapAB activity in a narrow window of potential. This behaviour is resistant to change of pH, nitrate concentration and inhibitor concentration and its possible mechanistic origins are discussed.

A Study of the Colorimetric Dinitrophenylhydrazine Method for the Determination of Serum Glutamic Oxalacetic Transaminase Activity

1966 ◽  
Vol 12 (4) ◽  
pp. 217-225 ◽  
Author(s):  
J S Annino
Keyword(s):  
Enzyme Activity ◽  
Transaminase Activity ◽  
Reagent Blank ◽  
Glutamic Oxalacetic Transaminase ◽  
Color Development ◽  
High Enzyme ◽  
Serum Glutamic Oxalacetic Transaminase ◽  
The Relationship ◽  
High Enzyme Activity

Abstract Study of the colorimetric transaminase method of Reitman and Frankel for the determination of serum glutamic oxalacetic transaminase activity revealed the following: (1) although maximum absorption occurs at 444 mµ, absorbance readings at 505 mµ gave satisfactory results; (2) color development is immediate and the color is stable for at least 1 hr.; (3) a pyruvate calibration standard may be used; (4) sample blanks are not usually necessary; (5) a reagent blank should accompany each group of analyses and should be used as a photometric reference; (6) the relationship between dilution and enzyme activity is linear; and (7) although the relationship between incubation time and activity is not exactly linear, a factor has been determined to permit the use of a 12-min. incubation period with samples showing high enzyme activity.

scholarly journals Peroxidase activity in human cutaneous mast cells: an ultrastructural demonstration.

1984 ◽  
Vol 32 (6) ◽  
pp. 573-578 ◽  
Author(s):  
L M Escribano ◽  
L C Gabriel ◽  
T Sainz ◽  
A Rocamora ◽  
J M Arrazola ◽  
...  
Keyword(s):  
Mast Cell ◽  
Enzyme Activity ◽  
Mast Cells ◽  
Peroxidase Activity ◽  
Ultrastructural Level ◽  
Prostaglandin Synthesis ◽  
Cell Disease ◽  
Mast Cell Disease ◽  
Cytochemical Technique ◽  
The Relationship

An intense and reproducible peroxidase staining in the cutaneous mast cells of two patients with systemic mast cell disease and urticaria pigmentosa is demonstrated at the ultrastructural level. This enzyme activity was demonstrated by use of a cytochemical technique employing 3,3'- diaminobenzicine (DAB) as an oxidizable substrate, after fixation by a tannic acid-aldehyde mixture. Enzyme activity was localized in the perinuclear cisterna and strands of endoplasmic reticulum. Granules appeared unreactive. This peroxidase activity appears sensitive to fixation by aldehydes; it is inhibited by 3-amino-1,2,4-triazole (AMT) and by lack of H2O2 or DAB in the incubation medium. These characteristics are fundamentally different from the peroxidase activity of basophils, and the demonstration of this enzyme is therefore not a further argument for a common ontogenetic origin of both cells. On the other hand, the cytochemical characteristics of this enzyme are very similar to those of platelet peroxidase (P-PO), which has been connected to the synthesis by platelets of prostaglandins. Since the mast cell is known to generate prostaglandins, the relationship between the enzyme described and prostaglandin synthesis by mast cells is discussed.

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