Effect of phospholipase A on the structure & function of yeast Candida albicans
Trivedi, A.; Singh, M.; Khare, S.; Singhal, G.S.; Prasad, R.
Indian Journal of Biochemistry and Biophysics 19(5): 336-341
1982
ISSN/ISBN: 0301-1208 PMID: 6764210 Document Number: 193623
The partially purified phospholipase A was not freely accessible to the membrane phospholipids of C. albicans. The phospholipase A-treated spheroplasts showed that phosphatidylethanolamine and phosphatidylserine plus phosphatidylinositol were cleaved by 40 and 50% respectively, while phosphatidylcholine was only 20% hydrolyzed. The uptake of several amino acids was enhanced in phospholipase A-treated spheroplasts, which was associated with a change in the apparent Km values. The relative fluorescence intensity of 1-anilino-8-naphthalene sulphonate (ANS) was less in phospholipase A-treated spheroplasts. The decrease in the fluorescence was due to a change in the apparent dissociation constant (Kd) of the dye-membrane complex, and a decrease in the number of irreversible and/or slowly reversible binding sites (n ). The potential value of enzymatic phospholipid cleavage to probe the lipid dependency of mediated transport processes in yeast membrane was demonstrated.