T. Genomic DNA was eluted in 50 ml of Tris-EDTA (TE) buffer. Fifty microliters of DNA option was ready from the 3 kinds of samples. DNA concentration was measured utilizing a UV spectrophotometer and converted to the amount of DNA per solution volume. The DNA concentration was 0.5/1000.7/ 1000. H E section preparation. Specimens were fixed with ten formalin, embedded in paraffin, and sectioned at a thickness of 20 mm. The tissue sections were stained with H E and observed under an optical microscope to confirm the tissue diagnosis. The tissue sections have been then examined by confocal Raman spectroscopy. Tissue preparation. Fresh biopsy specimens collected in the course of gastroscopy from either gastric cancer or regular gastric mucosa have been stored in 1.8-ml sterile vials kept on ice and transported for the Raman spectrometry laboratory (Raman spectrometry was performed within 1 h of tissue removal).Raman spectrometrySurface-enhanced Raman spectrometry of genomic DNA. RENISHAW confocal Raman spectrometry was usedwith a He-Ne laser. The excitation wavelength was 632.eight nm, plus the power was 5 mW. The integration time was 10 s63, and thePLOS A single | www.plosone.orgRaman Spectroscopy of Malignant Gastric MucosaTable 1. Tentative assignments of Raman bands (human tissue).Position of character peak 622 645 669 721 758 786 829 855 877 938 957 1001004 1033 1065 1083095 1127 1157.00 1173 1209 1230240 1245255 1264272 1266 1288304 1320Biochemical Assignments dc-c (Twisted) phenylalanine dC dT dA ns (Indole ring breathing) nsPO2- group nasPO2n n nC-C C-C C-CBiomolecular Assignments Phenylalanine, Tyrosine Nucleic acid Nucleic acid Nucleic acid Tryptophan DNA, RNA Nucleic acid Protein (collagen) Protein (collagen) Protein (collagen) Lipid, protein Phenylalanine, protein Phenylalanine, tryptophan, tyrosineProline Hydroxyproline Proline and valine (a-helix)dCH3 (deformed) n ring breathing dC-H (Plane bending) aromatic compound n-C = C = C-O-P-O-,ns nvC-CphospholipidC-CNucleic acid (DNA, RNA) Protein, Lipid Carotenoids Phenylalanine, tyrosine (protein) Tryptophan, phenylalanine (protein)C-Nprotein, vlipidPolyene chain dC-H (In-plane bending) phenylalanine, tyrosine nC-C6HTryptophan and phenylalanineAmino compound III (b fold) Amino compound III (random coil, corner) Amino compound III (a-helix) nC-Hand dH-N- (Bending) amino compound IIIProteinLipid ch2 bending vibration and bending vibration ch2ch3 nCh2chand dCh2ch3 (Swing) proteins and nucleic acidsProtein, nucleic acid Unsaturated fatty acid Protein, Lipid CarotenoiddC-H (Plane deformation) ordinary olefin 1448 1527 1551 1585 1605 1617 1640-1680 dCH2 (Bending) proteins and lipids nC-CCarotenoidsnas-NOn c = c Lipid n nC=C C=CUnsaturated fatty acid Phenylalanine, tyrosine Porphyrin and tryptophan ProteinAromatic compoundAmino compounds I, a helixn: stretching vibration, nas: asymmetric stretching vibration, ns: symmetric stretching vibration, d: bending, deformed, swing (relative peak intensity = the peak intensity/ typical intensity with the complete spectrum).Brassinolide doi:10.Orlistat 1371/journal.PMID:23805407 pone.0093906.tresolution was 1 cm-1. Twenty microliters of DNA solution was loaded on each slide, and 20 ml of DNA remedy from cancer cells was loaded on an enhanced matrix. The Raman spectrum was then analyzed. The scanning range was 400000 cm-1. The principle for confocal Raman spectrometry is illustrated in Figure 1. Through the examination, the sample was placed at the focal plane of the objective. The excitation laser was focused throug.
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