Abstract:
:A human, 85-kDa arachidonoyl-specific, cytosolic phospholipase A2 was expressed using the baculovirus-insect cell expression system. Expression resulted in the production of an active protein which consisted of approximately 3% of the total protein in the host Spodoptera frugiperda (Sf9) cells at 67 h after infection. The phospholipase A2 was purified to apparent homogeneity and exhibited calcium-dependent phospholipase A2 activity with a specific activity of 8 mumol/min/mg protein, as well as calcium-independent lysophospholipase activity with a specific activity of 17 mumol/min/mg protein. The phospholipase A2 was expressed as a phosphoprotein and was primarily phosphorylated on serine residues. Phosphatase treatment of the recombinant phospholipase A2 resulted in dephosphorylation of the enzyme and a 63% decrease in phospholipase A2 activity. This decrease in activity is similar in magnitude to the decrease in activity observed with phosphatase-treated phospholipase A2 from stimulated mammalian cells. These data demonstrate that the 85-kDa phospholipase A2 is expressed as an activated phosphoprotein in Sf9 cells.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
de Carvalho MS,McCormack FX,Leslie CCdoi
10.1006/abbi.1993.1549subject
Has Abstractpub_date
1993-11-01 00:00:00pages
534-40issue
2eissn
0003-9861issn
1096-0384pii
S0003986183715493journal_volume
306pub_type
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