A new kinetic method is described for the assay of quinone-reducing enzymes in various biological materials. It is based on polarographic determination of oxygen uptake in spontaneous oxidation of the diphenol formed as a result of 4-anilino-5-methoxybenzoquinone-1 ,2 (AMOBQ) enzymic reduction. The
A method for rapid enzyme kinetic assays at increased hydrostatic pressure
โ Scribed by K.C. Mohankumar; L.R. Berger
- Publisher
- Elsevier Science
- Year
- 1972
- Tongue
- English
- Weight
- 413 KB
- Volume
- 49
- Category
- Article
- ISSN
- 0003-2697
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โฆ Synopsis
A stainless-steel cylindrical vessel is described with optical ports which can be pressurized to 1000 atm (hydrostatic).
Constituents for enzymic reactions are injected directly into the vessel, sealed without use of tools, and pressurized. All these operations can be completed in about 10 sec. The vessel fits in the optical path of a spectrophotometer; continuous readout of the progress of the reaction is recorded. Complete reactions may be flushed from the cylinder and a new reaction initiated within a minute. A wide range of modifications of the apparatus is possible. Operation of the apparatus is demonstrated using operation of the enzymic hydrolysis of pnitrophenyl phosphate as model system.
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