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Action of trypanosomal lipolytic enzymes on the membrane-form variant surface glycoprotein of trypanosoma brucei

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6986117

The membrane-form variant surface glycoprotein (mfVSG) of Trypanosoma brucei is anchored in the plasma membrane by myristoyl residues ester-linked to glycerophosphoethanolamine. The authors have extracted (myristoyl-/sup 3/H)-mfVSG from trypanosomes incubated with (/sup 3/H)-myristate and have isolated the protein by reverse phase HPLC. The extraction solvent, 20% acetonitrile in 0.1% trifluoroacetic acid, prevents lipolysis of the mfVSG during isolation. The mfVSG was shown to be homogeneous by SDS-PAGE, with an apparent molecular mass ratio of 66,000. No other proteins were labelled with (/sup 3/H)-myristate. The major lipolytic enzyme of T. brucei, phospholipase A/sub 1/, did not release myristate from mfVSG to any significant extent, though the enzyme readily hydrolyzes ester linkages of myristoyl phospholipids and p-nitrophenylmyristate. Trypanosomal membranes contain a phosphodiesterase which releases (/sup 3/H)-1,2-diglyceride from (/sup 3/H)-myristoyl-mfVSG. The phospholipase A/sub 1/ can be separated from the myristoyl-releasing activity (phosphodiesterase) by centrifugation, affinity chromatography and anion-exchange chromatography.

Research Organization:
Guelph-Waterloo Centre for Graduate Work in Chemistry, Ontario
OSTI ID:
6986117
Report Number(s):
CONF-8606151-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Vol. 45:6; ISSN FEPRA
Country of Publication:
United States
Language:
English