Literature DB >> 11280970

Cyanide-induced alterations to the biophysical conformations of the isolated fish liver.

Y D Cheng1, T Y Liu, S Y Lin.   

Abstract

The purpose of this study is to examine the applicability of an infared spectroscopic methodology for the study of an environmental problem. The effect of cyanide concentrations on the biophysical conformation of the fish liver homogenate was determined by using an attenuated total reflectance (ATR)/Fourier transform infrared (FT-IR) microspectroscopy. Alive male model fish, Tilapia Zillii, was used. The liver from fish was isolated and homogenized in pH 8.0 Tris buffer solution. The results indicate that the IR peak intensity increased markedly in the C-H stretching range (3000-2800 cm-1), ester C = O stretching of lipids (1743 cm-1) and carbohydrate bands (1195-950 cm-1), but decreased in the amide I at 1649 cm-1 and the free asymmetric stretching band of phosphate at 1261 cm-1 with the increase of KCN concentrations. The marked release of hepatic enzymes and glutathione into homogenate induced by cyanide might account for the higher IR spectral peak intensity of fish liver tissue after treatment with KCN. The cyanide was also found to induce the protein structure of fish liver homogenate from alpha-helical conformation to beta-conformation.

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Year:  2001        PMID: 11280970     DOI: 10.1023/a:1008962907875

Source DB:  PubMed          Journal:  Ecotoxicology        ISSN: 0963-9292            Impact factor:   2.823


  14 in total

1.  pH-dependent secondary conformation of the peptide hormone leptin in different buffer solutions.

Authors:  L C Au; S Y Lin; M J Li; C J Ho
Journal:  Artif Cells Blood Substit Immobil Biotechnol       Date:  1999-03

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Authors:  J L WOOD; S L COOLEY
Journal:  J Biol Chem       Date:  1956-01       Impact factor: 5.157

3.  The in vivo inactivation by cyanide of brain cytochrome oxidase and its effect on glycolysis and on the high energy phosphorus compounds in brain.

Authors:  H G ALBAUM; J TEPPERMAN; O BODANSKY
Journal:  J Biol Chem       Date:  1946-07       Impact factor: 5.157

4.  Fourier transform infrared spectral evidences for protein conformational changes in immature cataractous human lens capsules accelerated by myopia and/or systemic hypertension.

Authors:  S Y Lin; S M Lee; M J Li; R C Liang
Journal:  Spectrochim Acta A Mol Biomol Spectrosc       Date:  1997-08       Impact factor: 4.098

5.  Thermal stability and reversibility of secondary conformation of alpha-crystallin membrane during repeated heating processes.

Authors:  S Y Lin; C J Ho; M J Li
Journal:  Biophys Chem       Date:  1998-08-04       Impact factor: 2.352

6.  pH-dependent secondary conformation of bovine lens alpha-crystallin: ATR infrared spectroscopic study with second-derivative analysis.

Authors:  S Y Lin; M J Li; C J Ho
Journal:  Graefes Arch Clin Exp Ophthalmol       Date:  1999-02       Impact factor: 3.117

Review 7.  Infrared spectroscopic studies of biomembranes and model membranes.

Authors:  D C Lee; D Chapman
Journal:  Biosci Rep       Date:  1986-03       Impact factor: 3.840

Review 8.  The use and misuse of FTIR spectroscopy in the determination of protein structure.

Authors:  M Jackson; H H Mantsch
Journal:  Crit Rev Biochem Mol Biol       Date:  1995       Impact factor: 8.250

9.  Studies of amygdalin (laetrile) toxicity in rodents.

Authors:  J D Khandekar; H Edelman
Journal:  JAMA       Date:  1979-07-13       Impact factor: 56.272

10.  Cyanide-induced injury to the isolated perfused rat liver.

Authors:  M Younes; O Strubelt
Journal:  Pharmacol Toxicol       Date:  1988-11
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