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
Partial purification and some properties of lipoxygenase fromSaccharomyces cerevisiae
β Scribed by B. Bisakowski; S. Kermasha; C. Schuepp
- Publisher
- Springer
- Year
- 1995
- Tongue
- English
- Weight
- 236 KB
- Volume
- 11
- Category
- Article
- ISSN
- 1573-0972
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β¦ Synopsis
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 demonstrated highest substrate specificity towards linoleic acid, followed by linolenic acid; although the enzyme had less specificity towards mono-linolein than di-linolein at pH 8.0, the reverse was true at pH 10.0.
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## Abstract __o__βDiphenolase extracted from __Triticum aestivum__ (cv. Nettuno) and purified in various steps gave a 250βfold purification over the crude extract. This purified enzyme showed maximum relative activity towards 4βmethylcatechol, generally high or moderate activity towards diβ and pol