Ethanol metabolism in suspension cultured carrot cells

1991 ◽  
Vol 82 (1) ◽  
pp. 103-108
Author(s):  
P. Perata ◽  
A. Alpi
Keyword(s):  
Ethanol Metabolism ◽  
Carrot Cells

Ethanol metabolism in suspension cultured carrot cells

1991 ◽  
Vol 82 (1) ◽  
pp. 103-108 ◽  
Author(s):  
P. Perata ◽  
A. Alpi
Keyword(s):  
Ethanol Metabolism ◽  
Carrot Cells

Ethanol Metabolism in Vivo and the Role of Hepatic Microsomal Ethanol Oxidation

1972 ◽  
Vol 33 (3) ◽  
pp. 751-755 ◽  
Author(s):  
Mary K. Roach ◽  
Myrna Khan ◽  
Marguerite Knapp ◽  
W. N. Reese
Keyword(s):  
Ethanol Oxidation ◽  
Ethanol Metabolism

Acetolactate Synthase of Suspension-Cultured Carrot Cells Resistant to Bensulfuron Methyl.

1992 ◽  
Vol 37 (4) ◽  
pp. 296-300
Author(s):  
Kenji Usui ◽  
Jun-ichi Adachi ◽  
Srisom Suwangwong ◽  
Kozo Ishizuka
Keyword(s):  
Acetolactate Synthase ◽  
Carrot Cells

Polymorphisms in alcohol metabolizing genes ADH2 and ADH3 and susceptibility to pancreatitis in alcoholics

2017 ◽  
Vol 6 (03) ◽  
pp. 5297
Author(s):  
Vedangi Aaren* ◽  
Godi Sudhakar ◽  
Girinadh L.R.S.
Keyword(s):  
Frequency Distribution ◽  
Ethanol Metabolism ◽  
Alcoholic Pancreatitis ◽  
Cytochrome P450 Enzyme ◽  
Increased Risk ◽  
Significant Difference ◽  
Pcr Rflp ◽  
P450 Enzyme ◽  
Acute Alcoholic Pancreatitis ◽  
Acute And Chronic Pancreatitis

In both developed and developing countries, overuse of alcohol is a considered as the major cause of acute and chronic pancreatitis. Prolonged overconsumption of alcohol for 5–10 years typically precedes the initial attack of acute alcoholic pancreatitis. It is observed that only a minority (around 5%) of alcoholics develop pancreatitis. It is now established that the pancreas has the capacity to metabolize ethanol. Previous studies have shown that there are two major pathways of ethanol metabolism, oxidative and non-oxidative. Oxidative ethanol metabolism involves the conversion of ethanol to acetaldehyde, a reaction that is catalysed by aldehyde dehydrogenase (ADH) with contributions from cytochrome P450 enzyme (CYP2E1) and possibly also catalase. Genetic factors regulating alcohol metabolism could predispose in developing alcoholic pancreatitis (AP). We investigated the association of polymorphisms in ADH enzymes with the alcoholic pancreatitis in North coastal Andhra Pradesh. Patients with alcoholic pancreatitis (AP; n = 100), alcoholic controls (AC; n = 100), and healthy controls (HC; n = 100) were included in the study. Blood samples were collected from the subjects in EDTA coated vials. DNA was extracted and genotyping for ADH2 and ADH3 was done by PCR-RFLP (polymerase chain reaction restriction fragment length polymorphism). The products were analysed by gel electrophoresis. The frequency distribution of ADH3*1/*1 genotype was significantly higher in AP group (54%) compared with AC (35%), and HC (42%), and was found to be associated with increased risk of alcoholic pancreatitis. There was no statistically significant difference between the frequency distribution of ADH3*1/*1, ADH3*1/*2, and ADH3*2/*2 genotypes between AC and HC. There was no statistically significant difference between the frequency distribution of ADH2*1/*1, ADH2*1/*2, and ADH2*2/*2 genotypes in AP compared with AC and HC. This study shows that carriers of ADH3*1/*1 individuals consuming alcohol are at higher risk for alcoholic pancreatitis than those with other genotypes such as ADH3*1/*2 and ADH3*2/*2. 

scholarly journals Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the corresponding cDNA

1997 ◽  
Vol 325 (3) ◽  
pp. 761-769 ◽  
Author(s):  
Isabelle GARCIA ◽  
Matthew RODGERS ◽  
Catherine LENNE ◽  
Anne ROLLAND ◽  
Alain SAILLAND ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Gel Filtration ◽  
Peptide Sequence ◽  
Amino Acid Residues ◽  
Carrot Cells ◽  
Expression Studies ◽  
Sds Page ◽  
Molecular Masses ◽  
The Difference ◽  
Dioxygenase Activity

p-Hydroxyphenylpyruvate dioxygenase catalyses the transformation of p-hydroxyphenylpyruvate into homogentisate. In plants this enzyme has a crucial role because homogentisate is the aromatic precursor of all prenylquinones. Furthermore this enzyme was recently identified as the molecular target for new families of potent herbicides. In this study we examine precisely the localization of p-hydroxyphenylpyruvate dioxygenase activity within carrot cells. Our results provide evidence that, in cultured carrot cells, p-hydroxyphenylpyruvate dioxygenase is associated with the cytosol. Purification and SDS/PAGE analysis of this enzyme revealed that its activity is associated with a polypeptide of 45–46 kDa. This protein specifically cross-reacts with an antiserum raised against the p-hydroxyphenylpyruvate dioxygenase of Pseudomonas fluorescens. Gel-filtration chromatography indicates that the enzyme behaves as a homodimer. We also report the isolation and nucleotide sequence of a cDNA encoding a carrot p-hydroxyphenylpyruvate dioxygenase. The nucleotide sequence (1684 bp) encodes a protein of 442 amino acid residues with a molecular mass of 48094 Da and shows specific C-terminal regions of similarity with other p-hydroxyphenylpyruvate dioxygenases. This cDNA encodes a functional p-hydroxyphenylpyruvate dioxygenase, as evidenced by expression studies with transformed Escherichia coli cells. Comparison of the N-terminal sequence of the 45–46 kDa polypeptide purified from carrot cells with the deduced peptide sequence of the cDNA confirms that this polypeptide supports p-hydroxyphenylpyruvate dioxygenase activity. Immunodetection studies of the native enzyme in carrot cellular extracts reveal that N-terminal proteolysis occurs during the process of purification. This proteolysis explains the difference in molecular masses between the purified protein and the deduced polypeptide.

scholarly journals Dehydrogenase-dependent Ethanol Metabolism in Deer Mice (Peromyscus maniculatus) Lacking Cytosolic Alcohol Dehydrogenase

1989 ◽  
Vol 264 (10) ◽  
pp. 5593-5597
Author(s):  
C Norsten ◽  
T Cronholm ◽  
G Ekström ◽  
J A Handler ◽  
R G Thurman ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Peromyscus Maniculatus ◽  
Ethanol Metabolism ◽  
Deer Mice

scholarly journals The Rate of Ethanol Metabolism in Fed and Fasting Animals

1959 ◽  
Vol 234 (6) ◽  
pp. 1544-1549
Author(s):  
Marion Edmonds Smith ◽  
Henry Wise Newman
Keyword(s):  
Ethanol Metabolism

In vivo protective effect against ethanol metabolism and liver injury of oyster (Crassostrea Gigas) extracts obtained via subcritical water processing

2021 ◽  
Author(s):  
Hee-Jeong Lee ◽  
Periaswamy Sivagnanam Saravana ◽  
Truc Cong Ho ◽  
Yeon-Jin Cho ◽  
Jin-Seok Park ◽  
...  
Keyword(s):  
Liver Injury ◽  
Protective Effect ◽  
Crassostrea Gigas ◽  
Subcritical Water ◽  
Ethanol Metabolism

scholarly journals Identification and Functional Analysis of ThADH1 and ThADH4 Genes Involved in Tolerance to Waterlogging Stress in Taxodium hybrid ‘Zhongshanshan 406’

Genes ◽  
2021 ◽  
Vol 12 (2) ◽  
pp. 225
Author(s):  
Lei Xuan ◽  
Jianfeng Hua ◽  
Fan Zhang ◽  
Zhiquan Wang ◽  
Xiaoxiao Pei ◽  
...  
Keyword(s):  
Ethanol Metabolism ◽  
Flooding Tolerance ◽  
Transcriptome Data ◽  
Low Oxygen ◽  
Anaerobic Conditions ◽  
Waterlogging Tolerance ◽  
Waterlogging Stress ◽  
Adh Genes ◽  
Oxygen Conditions ◽  
Stems And Leaves

The Taxodium hybrid ‘Zhongshanshan 406’ (T. hybrid ‘Zhongshanshan 406’) [Taxodium mucronatum Tenore × Taxodium distichum (L.). Rich] has an outstanding advantage in flooding tolerance and thus has been widely used in wetland afforestation in China. Alcohol dehydrogenase genes (ADHs) played key roles in ethanol metabolism to maintain energy supply for plants in low-oxygen conditions. Two ADH genes were isolated and characterized—ThADH1 and ThADH4 (GenBank ID: AWL83216 and AWL83217—basing on the transcriptome data of T. hybrid ‘Zhongshanshan 406’ grown under waterlogging stress. Then the functions of these two genes were investigated through transient expression and overexpression. The results showed that the ThADH1 and ThADH4 proteins both fall under ADH III subfamily. ThADH1 was localized in the cytoplasm and nucleus, whereas ThADH4 was only localized in the cytoplasm. The expression of the two genes was stimulated by waterlogging and the expression level in roots was significantly higher than those in stems and leaves. The respective overexpression of ThADH1 and ThADH4 in Populus caused the opposite phenotype, while waterlogging tolerance of the two transgenic Populus significantly improved. Collectively, these results indicated that genes ThADH1 and ThADH4 were involved in the tolerance and adaptation to anaerobic conditions in T. hybrid ‘Zhongshanshan 406’.

Ether Inhibition of Ethanol Metabolism in Isolated Rat Liver Parenchymal Cells

1981 ◽  
Vol 5 (4) ◽  
pp. 550-555 ◽  
Author(s):  
Hakon Aune ◽  
Allan R. Stowell ◽  
Jorg Morland
Keyword(s):  
Rat Liver ◽  
Ethanol Metabolism ◽  
Liver Parenchymal ◽  
Isolated Rat Liver ◽  
Parenchymal Cells ◽  
Isolated Rat
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