G. Gilljam et al., PURIFICATION OF SIMIAN IMMUNODEFICIENCY VIRUS, SIVMAC251, AND OF ITS EXTERNAL ENVELOPE GLYCOPROTEIN, GP148, Journal of chromatography, 675(1-2), 1994, pp. 89-100
Two-phase extraction in a system composed of dextran and polyethylene
glycol was used to purify simian immunodeficiency virus, SIVMAC251 (32
H isolate) from 25 l of culture supernatant. The virus partitioned to
the interphase with 80% recovery of gag peptide p27 and reverse transc
riptase and an about 25% recovery of the external env glycoprotein, gp
148. The virus was treated with octylglycoside and its subcomponents s
eparated. Two gag-p27 containing,fractions were obtained; gag-1, which
also contained reverse transcriptase and nucleopeptides, and gag-2, w
hich contained the major portion of the p27. The env gp148 was purifie
d by chromatography through a series of lectin columns. The prepared m
aterials are characterized by sodium dodecyl sulphate-polyacrylamide g
el electrophoresis and immuno- and lectin blotting.