A modified procedure for studying enzyme secretion in yeast sphaeroplasts: subcellular distribution of invertase
- 1 July 1976
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Microbiology
- Vol. 22 (7), 989-995
- https://doi.org/10.1139/m76-144
Abstract
A significantly modified procedure for investigating enzyme secretion from yeast sphaeroplasts, and results from its application are described. Sphaeroplasts were derepressed for invertase biosynthesis in the presence of helicase and fractionated to reveal the distribution of high and low molecular weight forms of invertase. Secreted enzyme was found to be of high molecular weight, exclusively. Less than 10% of the total invertase activity was present in washed sphaeroplasts and of this, 43% was soluble, consisting of both high and low molecular weight forms of invertase. Washed membranes retained 32% of the internal invertase activity, and on solubilization with Triton X-100 the enzyme was found to be of an intermediate molecular weight. These results are consistent with the hypothesis that invertase is glycosylated at the plasma membrane.This publication has 2 references indexed in Scilit:
- Comparative Study of the Properties of the Purified Internal and External Invertases from YeastJournal of Biological Chemistry, 1968
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951