Abstract:
: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.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Tsirka SA,Kyriakidis DAdoi
10.1007/BF00226142subject
Has Abstractpub_date
1988-10-01 00:00:00pages
147-55issue
2eissn
0300-8177issn
1573-4919journal_volume
83pub_type
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