“…The protein concentrations were accurately measured spectroscopically using the e 280 values as follows: BSA, 6.6; HSA, 5.3; human IgG, 13.8; fibrinogen, 15.1; transferrin, 11.2 and haemoglobin, 694.4 at 280 nm. 15 Stock standard solutions of the dyes (1.0 3 10 23 mol l 21 ), Rose Bengal (CI 45440), fluorescein (CI 45350), dichlorofluorescein (CI 45365), Eosin B (CI 45400), Eosin Y (CI 45380), Erythrosine B (CI 45430) and floxin (CI 45410) were prepared by dissolving the appropriate amount of the acid form of the dye (Sigma) in 0.02 mol l 21 sodium hydroxide solution and diluting with water to 250 ml. These solutions were kept in amber-coloured bottles in the dark.…”
The stopped-flow mixing technique was used to develop a very fast, sensitive and accurate method for determining total proteins. The method is based on the lower fluorescence of Rose Bengal caused by binding of the dye to the proteins. The decrease in the fluorescence intensity, measured at 572 nm with excitation 555 nm, was linearly related to protein concentration from 1.3 to 24.5 micrograms ml-1. The detection limit was 0.3 microgram ml-1. The method was satisfactorily applied to the determination of total proteins in different serum samples.
“…The protein concentrations were accurately measured spectroscopically using the e 280 values as follows: BSA, 6.6; HSA, 5.3; human IgG, 13.8; fibrinogen, 15.1; transferrin, 11.2 and haemoglobin, 694.4 at 280 nm. 15 Stock standard solutions of the dyes (1.0 3 10 23 mol l 21 ), Rose Bengal (CI 45440), fluorescein (CI 45350), dichlorofluorescein (CI 45365), Eosin B (CI 45400), Eosin Y (CI 45380), Erythrosine B (CI 45430) and floxin (CI 45410) were prepared by dissolving the appropriate amount of the acid form of the dye (Sigma) in 0.02 mol l 21 sodium hydroxide solution and diluting with water to 250 ml. These solutions were kept in amber-coloured bottles in the dark.…”
The stopped-flow mixing technique was used to develop a very fast, sensitive and accurate method for determining total proteins. The method is based on the lower fluorescence of Rose Bengal caused by binding of the dye to the proteins. The decrease in the fluorescence intensity, measured at 572 nm with excitation 555 nm, was linearly related to protein concentration from 1.3 to 24.5 micrograms ml-1. The detection limit was 0.3 microgram ml-1. The method was satisfactorily applied to the determination of total proteins in different serum samples.
“…Figure 4(A) shows the UV–vis spectra of gelatin and PVA homopolymers. The general characteristic of both spectra were that they are composed of an almost flat baseline (absorption negligible) and a steep rise near the absorption edge (remarkable absorption), 22. The spectrum of pure gelatin film had an intense band at about 210 nm, which may have been due to the presence of chromophoric groups.…”
Differential scanning calorimetry, thermogravimetric analysis, X-ray diffraction, and ultraviolet-visible spectroscopy of gelatin and poly(vinyl alcohol) (PVA) homopolymers and their blended samples were studied. The data revealed that the gelatin and PVA polymers were compatible over the investigated range of compositions; this contributed to the formation of hydrogen-bonding interaction between their polar groups. The associated enthalpy-ofmelting transition and thermal stability of the blended samples increased with increasing PVA content. This indicated that the crystalline structure of PVA was not destroyed completely in the blends, which was consistent with the X-ray diffraction pattern of the 50/50 (wt %/wt %) blended gelatin/PVA sample. The absorption edge and optical band gap for allowed direct transition were determined from ultraviolet-visible spectra. The induced changes in the band structure are elucidated. V C 2010 Wiley Periodicals, Inc. J Appl Polym Sci 118: [413][414][415][416][417][418][419][420] 2010
“…This theory is supported by a recent study showing that the corneal epithelium absorbs UVC very effectively and absorbs the shorter wavelength range of UVB (280–300 nm) quite well (33, 34). It has been suggested that tryptophan and tyrosine residues within protein may be responsible for UVB absorption, as these amino acids have a maximum absorption at 280–290 nm (37). Uric acid, an endogenous purine degradation product found in all cells, absorbs at 292 nm, and this may also help attenuate the level of UVB (38).…”
Ultraviolet (UV)‐mediated DNA damage in various tissues has been well documented. However, research on the damaging effect of UV irradiation on the DNA of corneal epithelium is scarce, even though this is of interest because the cornea is directly exposed to damaging solar (UV) radiation. In this study, we developed a corneal epithelium Comet assay model to to assess the background DNA damage (as strand breaks) n cells retrieved from different layers of the porcine corneal epithelium, and to investigated the effect of UV irradiation on DNA damage in corneal epithelial cells. Results show that the background DNA strand breaks decreased significantly (P < 0.001) toward deeper layers of the epithelium. Exposure to the same intensity (0.216 J/cm2) of UVA, UVB and UVC caused a significant (P < 0.001) increased in DNA strand breaks of deeper‐layer cells: mean ± SD %DNA scores (10 gels per treatment, with 100 irradiated cells scored per gel) were 10.2%± 1.4% for UVA, 27.4%± 4.6% for UVB, and 14.7%± 1.8% for UVC compared with 4.2%± 0.05% for controls (ambient room light). This study has shown for the first time that the Comet assay for DNA strand breaks can be used successfully with corneal epithelial cells. This report will support future studies investigating environmental influences on corneal health and the assessment of possible protective strategies, and in applying DNA lesion‐specific versions of the Comet assay in this corneal epithelial cell model.
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