2008
DOI: 10.1016/j.fct.2008.09.001
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Fourier transform infrared study of protein secondary structural changes in the muscle of Labeo rohita due to arsenic intoxication

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Cited by 46 publications
(42 citation statements)
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“…So, the sample was employed in 1 mg portions. Each 1 mg portion of sample was thoroughly mixed with 100 mg of completely dried potassium bromide (KBr) (Merck, Darmstadt, Germany; used without further purification), which is a ratio that is frequently used in the pellet technique employed in FTIR spectroscopy (Cakmak et al 2006;Dogan et al 2006;Garip et al 2007;Palaniappan and Vijayasundaram 2008). After mixing with the aid of an agate mortar and pestle, the mixtures were further dried for 1 hr to completely remove any trace of unbound water.…”
Section: Diel Vertical Migration Bioassaymentioning
confidence: 99%
See 1 more Smart Citation
“…So, the sample was employed in 1 mg portions. Each 1 mg portion of sample was thoroughly mixed with 100 mg of completely dried potassium bromide (KBr) (Merck, Darmstadt, Germany; used without further purification), which is a ratio that is frequently used in the pellet technique employed in FTIR spectroscopy (Cakmak et al 2006;Dogan et al 2006;Garip et al 2007;Palaniappan and Vijayasundaram 2008). After mixing with the aid of an agate mortar and pestle, the mixtures were further dried for 1 hr to completely remove any trace of unbound water.…”
Section: Diel Vertical Migration Bioassaymentioning
confidence: 99%
“…Vibrational bands are extremely sensitive to changes in chemical structure, conformation, and their environment (Freifelder 1982;Stuart 1997). Fourier transform infrared (FTIR) Spectroscopy is a powerful tool for the molecular characterization-structurally and functionally-of biomolecules such as lipids, peptides, proteins, nucleic acids, and carbohydrates in a variety of samples including bacteria, plant materials, animal tissues, and foodstuff (Giordano et al 2001;Cakmak et al 2006;Garip et al 2007;Palaniappan and Vijayasundaram 2008). The foremost advantage of FTIR spectroscopy is its ability to present an overall 'organic chemical fingerprint' based on vibrational features of the macromolecular pool of the sample without its destruction.…”
Section: Introductionmentioning
confidence: 99%
“…Similarly, changes in the intensity of phospodiester band at ~1088 cm -1 showed an increase in the content of nucleic acids of liver but decrease in muscle. Previously a decrease in the nucleic acid content was also observed in the arsenic intoxicated brain tissue of Labeo rohita (Palaniappan and Vijayasundaram 2008). Significant changes in the band areas at 3307, 1543, 1163, 696 of liver tissue and 3364, 2926, 1741, 1653, 1543, 1456, 1394, 1163 of muscles tissue further suggested that Cd had more drastic effect on the tissue architecture as compared to Pb.…”
Section: Discussionmentioning
confidence: 92%
“…The non-specific effects of As consist of a denaturation of proteins caused by hydrogen bond transitions and protein unfolding, involving the Amide I and Amide II bands of proteins [25][26][27][28][29]. As shown in Figure 7, this transition/denaturation is clearly linked to the modification of the β-sheet band at 1632 cm −1 present in the control sample and absent in the exposed sample.…”
Section: Non Specific Structural Changes Detected By Ftir Spectroscopmentioning
confidence: 94%
“…This spectral range has plenty of information about protein structures [24]. By determining the second derivative of the FTIR spectra in the 1700 to 1620 cm −1 sub-range, the changes in the secondary protein structures involving alpha helix, beta sheet, beta turn, and random coil transitions can also be detected [5,14,[25][26][27][28] Moreover, the changes of the ratio between the 1580-1520 cm −1 and the 1700-1580 cm −1 (PO) sub-ranges evidence protein depletion and oxidation [3,14,28,29]. The fatty acid range between 1700 and 1750 cm −1 (already described), when joined to the 1700 to 1620 cm −1 Amide I range of proteins, is also used to determine the lipid to protein ratio (LPR) which is another marker of protein oxidation [20,21].…”
Section: Ftir Spectroscopymentioning
confidence: 99%