Lab-Expt
Rapid Microscale Isolation and Purification of Yeast Alcohol Dehydrogenase Using Cibacron Blue Affinity Chromatography
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Abstract
A rapid microscale procedure has been developed for the isolation and purification of yeast alcohol dehydrogenase. Glass beads are used for cytolysis, PEG precipitation for partial purification and a cibacron blue affinity column for the final step. A 27.5 fold purification can be achieved in 2 - 3 hours.
Keywords (Audience):
Upper-Division UndergraduateKeywords (Domain):
BiochemistryKeywords (Feature):
The Microscale LaboratoryKeywords (Pedagogy):
Hands-On Learning / ManipulativesKeywords (Subject):
Microscale LabCiting Articles
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This article has been cited by 2 ACS Journal articles (2 most recent appear below).

Kinetics of Alcohol Dehydrogenase-Catalyzed Oxidation of Ethanol Followed by Visible Spectroscopy
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Kestutis Bendinskas , Christopher DiJiacomo , Allison Krill and Ed VitzJournal of Chemical Education2005 82 (7), 1068A two-week biochemistry experiment was introduced in the second-semester general chemistry laboratory to study the oxidation of ethanol in vitro in the presence of the enzyme alcohol dehydrogenase (ADH). This reaction should pique student interest because ...

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Paul A. CraigJournal of Chemical Education1999 76 (8), 1130A Project-Oriented Biochemistry Laboratory Course
Paul A. CraigJournal of Chemical Education1999 76 (8), 1130A project-oriented laboratory course has been designed to introduce students to the study of biochemistry as it is practiced. The course is designed to be a capstone experience for students enrolled in a variety of majors at the Rochester Institute of ...
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History
- Received: August 03, 2009
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