Action of tryptophan analogues inSaccharomyces cerevisiae
✍ Scribed by Giuseppe Miozzari; Peter Niederberger; Ralf Hütter
- Book ID
- 104777661
- Publisher
- Springer
- Year
- 1977
- Tongue
- English
- Weight
- 989 KB
- Volume
- 115
- Category
- Article
- ISSN
- 0302-8933
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
The free tryptophan pool and the levels of two enzymes of tryptophan biosynthesis (anthranilate synthase and indoleglycerolphosphate synthase)have been determined in a wild type strain of Saccharomyces cerevisiae and in mutants with altered regulatory properties.
Tryptophan was found to be degraded in Saccharomyces cerevisiae mainly to tryptophol. Upon chromatography on DEAE-cellulose two aminotransferases were identified: Aromatic aminotransferase I was constitutively synthesized and was active in vitro with tryptophan, phenylalanine or tyrosine as amino do
Mitochondrial RNA from grande yeast was analyzed by electrophoresis on agarose-urea, acrylamide-urea, and methyl mercuric hydroxide-agarose gels. These gel systems display more than 40 RNA bands that copurify with mitochondria; these bands are not present in cytoplasmic RNA preparations. Analysis of
ary experiments indicate that this sensor may be applicable in short-term experiments on alcohol production by aerated yeast suspensions. Alcohol oxidase may also be used for colorimetric alcohol assays by an oxidase-peroxidase-ABTS method (cf. Bernt and Lachenicht, 1974). In this case, inactivatio