Effect of 4-methylpyrazole on ethanol-induced decrease in rat plasma amino acids.

M Hagman; R Jagenburg

doi:10.1016/0006-2952(89)90156-1

Home/Archive/PubMed

PubMed · 2910296

Effect of 4-methylpyrazole on ethanol-induced decrease in rat plasma amino acids.

M Hagman·R Jagenburg

View original source ↗Export metadata ↓

Abstract

It has been shown earlier that an acute dose of ethanol causes an immediate decrease in the concentration of most plasma amino acids, and that this decrease involves both beta-adrenergic and adrenocortical mechanisms. In this work is shown that the oxidation of ethanol also plays an important role in the amino acid decreasing effect. Male rats were pretreated with 4-methylpyrazole, an inhibitor of liver alcohol dehydrogenase, in doses causing an 85% inhibition of the ethanol elimination. In this group the ethanol-induced decrease in amino acids was much less pronounced than in a control group pretreated with saline.

Explore related subjects

Amino Acids Animals Ethanol Fomepizole Male Pyrazoles Rats Rats, Inbred Strains Journal Article Research Support, Non-U.S. Gov't

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

M Hagman, R Jagenburg. 1989-01-01. Effect of 4-methylpyrazole on ethanol-induced decrease in rat plasma amino acids.. https://doi.org/10.1016/0006-2952(89)90156-1

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2026

Chimeric structural isomer fragments as cost-efficient internal standards for amino acid quantification by mass spectrometry.

Amino acid (AA) profiles from body fluids such as blood and urine are clinical indicators for diagnosing metabolic and hepatic diseases. Current quantitative methods, such as liquid chromatography-mass spectrometry (LC-MS) with isotopically labelled internal standards (ISs), are costly and technically demanding. This study proposes a cost-efficient alternative using structural isomers as ISs in a direct liquid infusion (DLI) tandem mass spectrometry (MS/MS) approach. The method leverages chimeric spectra and fragment intensity ratios to quantify AAs, demonstrating high linearity and precision even with a 3D ion trap mass analyser. This approach offers a viable strategy for AA quantification in preventive medicine, particularly for screening metabolic diseases such as phenylketonuria, diabetes, and liver dysfunction.

Amino Acids↗

PubMed1992

A practical method for uniform isotopic labeling of recombinant proteins in mammalian cells.

A method to obtain uniformly isotopically labeled (15N and 15N/13C) protein from mammalian cells is described. The method involves preparation of isotopically labeled media consisting of amino acids isolated from bacterial and algal extracts supplemented with cysteine and enzymatically synthesized glutamine. The approach is demonstrated by producing 15N-labeled and 15N/13C-labeled urokinase from Sp2/0 cells and successfully growing Chinese hamster ovary (CHO) cells on the labeled media. Thus, using the procedures described, isotopically labeled proteins that have been expressed in mammalian cells can be prepared, allowing them to be studied by heteronuclear multidimensional NMR techniques.

Amino Acids↗

PubMed1992

A novel alpha-type fibrinogenase from Agkistrodon rhodostoma snake venom.

By means of CM-Sephadex C-50 column chromatography, gel-filtration on sephadex G-75 and Sephacryl S-200 columns, a purified fibrinogenase, kistomin, was obtained from venom of Agkistrodon rhodostoma. It was a single peptide-chain with a molecular mass of about 21,800 Da containing about 202 amino-acid residues as revealed by amino acid analysis. Kistomin preferentially cleaved A alpha- and subsequently the gamma-chain of fibrinogen, leaving the B beta-chain unaffected. Its fibrinogenolytic activity was estimated to be 36.6 +/- 4.5 mg/min per mg protein and was inhibited by the pretreatment of EDTA, suggesting that it is a metalloproteinase. Its fibrinogenolytic activity in platelet-poor plasma is much less potent as compared to that in purified fibrinogen solution. It inhibited ristocetin-induced aggregation of human platelets in a dose-dependent manner in the presence of von Willebrand factor.

Amino Acids↗