Analyses of viral proteins by SDS-gel electrophoresis on 11 % acrylamide gels. The amount of protein sample in each case was 7 μg. A. Conventional Coomassie blue-stained gel scanned at 620 nm. B. Fluorescence scan of gel containing protein labeled with fluorescamine.
Now you can combine the sensitivity and specificity of fluorescence with he convenience and performance of a Gilford Gel Scanner, b u Get Superior Results ensitivity is critical when you have only small mounts of sample: Gilford Fluorescence Gel canning offers 20 to 50 times the sensitivity of consntional techniques. Some proteins can be detected ι as little as one nanogram of material; quantitative jsults have been obtained from 5 to 200 nanograms of lyoglobin.
ou Get Faster Results ttra steps are eliminated: urinary proteins, for stance, can be detected from unconcentrated impies; in contrast, conventional electrophoresis
using Coomassie blue staining requires 25X sample concentration. For most tests, total analysis time is only a few hours, including electrophoresis. Even for compounds that cannot be tagged with fluorescence labeling, the Gilford Gel Scanner saves time, and it improves performance: high monochromatic energy, particularly in the UV, enhances spatial resolution by allowing narrower beam apertures. The scanner can resolve bands separated by as little as 0.05 mm. Fluorescence Gel Scanning is available in 10 or 20 cm scan lengths for any Gilford Spectrophotometer incorporating optical bench rods: this includes up dated DU® monochromators. 'Registered trademark of Beckman Corporation, Fullerton, CA
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Gilford Research Spectrophotometers: every job easier, every result more accurate ANALYTICAL CHEMISTRY, VOL. 50, NO. 11, SEPTEMBER 1978 · 961 A
