Cloning, Overexpression, and Purification of Cytosine Deaminase fromSaccharomyces cerevisiae
β Scribed by Martha S. Hayden; Peter S. Linsley; Alison R. Wallace; Hans Marquardt; David E. Kerr
- Book ID
- 115645269
- Publisher
- Elsevier Science
- Year
- 1998
- Tongue
- English
- Weight
- 351 KB
- Volume
- 12
- Category
- Article
- ISSN
- 1046-5928
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A homogenous polyphosphatase preparation was obtained from Saccharomyces cerevisiae cytosol with a 3β’8% yield and 3540-fold purification. The enzyme hydrolysed polyphosphate (polyP) with various chain lengths, including polyP 3 , and split P i off the end of the chain. It was inactive with respect t
A partially purified lipoxygenase extract was obtained from the yeast Saccharomyces cerevisiae by precipitation with solid (NH4)SO4 at 20% to 80% saturation. The enzyme had two pH optima, at pH 8.0 and 10.0, with respective apparent K m values of 13 and 9.5 ΞΌM. At both pH optima, the lipoxygenase de
Succinyl-CoA synthetase from Saccharomyces cerevisiae was partially purified (20-fold) with a yield of 44%. The Michaelis-Menten constants were determined: Km (succinate) = 17 mM; Km (ATP) = 0.13 mM; Km (CoA) = 0.03 mM. The succinyl-CoA synthetase has a molecular weight of about 80000 dalton (as det