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Studies on phospholipase activities inNeurospora crassaconidia

Authors
Journal
Archives of Biochemistry and Biophysics
0003-9861
Publisher
Elsevier
Publication Date
Volume
206
Issue
2
Identifiers
DOI: 10.1016/0003-9861(81)90106-5
Keywords
  • Lipids
Disciplines
  • Biology
  • Chemistry

Abstract

Abstract Phospholipase A activity has been characterized in the conidia of Neurospora crassa. It has been observed that almost the entire phospholipase A activity in the conidia could be leached out by washing these with aqueous solution. The properties of this exocellular phospholipase A have been determined. Two distinct phospholipases have been fractionated from the “conidial water washing” by gel chromatography using Sephadex G-100. Using specific substrate, 1-stearyl-2-oleoyl lecithin, the predominant phospholipase activity in the fraction with higher molecular weight has been found to be due to phospholipase A 1 and that in fraction with lower molecular weight has been found to be due to phospholipase A 2. Properties of these two different enzyme fractions have been studied. The most active fraction in the latter gives a single band in 7.5% polyacrylamide gel. Lysophospholipase activity and detergent-stimulated phospholipase D activity have been detected also in the conidia. The effects of different physical and chemical agents on phospholipase A activity in the “conidial water washing” as well as in the purified fractions have been studied.

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