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In vitroalterations of L-asparaginase activity ofTetrahymena pyriformisby lipids

✍ Scribed by Stella-Anna E. Tsirka; Dimitrios A. Kyriakidis

Publisher
Springer
Year
1988
Tongue
English
Weight
603 KB
Volume
83
Category
Article
ISSN
0300-8177

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✦ Synopsis

A membrane-bound L-asparaginase (EC 3.5.1.1) of Tetrahymena pyriformis was purified to homogeneity. The purified enzyme is a lipoprotein, since it is inactivated by phospholipase C and its activity is restored by the addition of naturally occurring lipids, such as phosphatidylcholine, triolein and oleyl acetate. The relative effectiveness of a variety of phospholipids, free saturated and unsaturated fatty acids, or neutral lipids, such as esters of fatty acids and glycerides, with respect to the activation of purified L-asparaginase is compared. Enzyme activity is reconstituted in the presence of lipids and evidence for the formation of an enzyme-phospholipid complex is presented. The data of this report suggest that L-asparaginase may have a requirement for lipids that reconstitute a physiological hydrophobic environment, similar to the one existing in vivo.

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