Detection of β-Glucosidase Activity in Polyacrylamide Gels with Esculin as Substrate
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چکیده
منابع مشابه
A Novel Method to Detect β-Cyclodextrin Glucosyl Transferase (β-CGTase) Activity on Polyacrylamide Gels
b-cyclodextrin glucosyl transferase (b-CGTase) hydrolyses starch to produce b-cyclodextrin by transglycosylation (cyclization) activity. The conventional method for detection of b-CGTase activity is based on detecting starch hydrolysis by iodine staining. This method reveals all amylolytic enzymes, but can not discriminate them. In the present study, we introduce a new method for specific detec...
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متن کاملa novel method to detect β-cyclodextrin glucosyl transferase (β-cgtase) activity on polyacrylamide gels
b-cyclodextrin glucosyl transferase (b-cgtase) hydrolyses starch to produce b-cyclodextrin by transglycosylation (cyclization) activity. the conventional method for detection of b-cgtase activity is based on detecting starch hydrolysis by iodine staining. this method reveals all amylolytic enzymes, but can not discriminate them. in the present study, we introduce a new method for specific detec...
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METHOD 1. Immerse the gel, together with its attached glass plate, in 7% acetic acid for 5 minutes. Remove the gel from the fixative by carefully lifting the glass plate from the fluid. 2. Rinse the gel briefly in deionized H2O. Remove excess fluid from the surface of the gel with a pad of Kimwipes. IMPORTANT Do not use absorbent paper; it will stick to the gel. 3. (Optional) Dry the gel onto a...
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A method for the detection and quantitation of unlabeled nucleic acids in polyacrylamide gels is presented. The technique is a variation on UV shadowing. The technique is based on the observation that some storage phosphor screens (Kodak in this case) are sensitive to UV light in the range where nucleic acids absorb most strongly. Nucleic acid present in a gel resting on the screen absorbs the ...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1994
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.60.12.4584-4586.1994