Purification of the photoreactivating enzyme from yeast
โ Scribed by Roger M. Herriott
- Publisher
- Elsevier Science
- Year
- 1979
- Tongue
- English
- Weight
- 427 KB
- Volume
- 95
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
A method for the rapid isolation of yeast enolases, yielding three distinct isoenzymes, has been devised. In the first step anionic proteins were precipitated with polyethyleneimine, whereas hydrophobic enolase isoenzymes remained in the supernatant. Secondly, the supernatant was 45% saturated with
Proteinase A was purified from commercial baker's yeast to homogeneity by using affinity chromatography. Simple and sensitive fluorometric assay procedures were developed for this enzyme, where Suc-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide and dimethylcasein were used as synthetic sub
The yeast Trichosporon adeninovorans secretes an amylase a t a high rate if grown in a medium containing starch or maltose. The enzyme was purified 29-fold by hydroxylapatite chromatography and gel filtration and characterized as a glucoamylase. The enzyme seems to be a glycoprotein with a molecular
## Abstract ฮฒโXylosidase activity has been detected in cellโfree extracts, in culture fluids and as cell wallโbound enzyme of __Arxula adeninivorans.__ With chromatographic procedures used to purify the activity two different forms of ฮฒโxylosidase (denoted ฮฒXโ1 and ฮฒXโ2) from the cellโfree extract