Studies of proteins soluble in acidic chloroform-methanol isolated from crude human leukocyte interferon preparations.
Acidic chloroform-methanol soluble proteins possessing hydrophobic properties and capable of inhibiting in vitro transcriptase activity of influenza virus RNP were detected in native and partially purified human leukocyte interferon (IFN) preparations. Purification of IFN resulted in the removal of at least a portion of such proteins; however, no proteins have been found in highly-purified IFN preparations.
Leneva
I A
IA
Mikhejeva
A V
AV
Kuznetsov
V P
VP
Seidel
W
W
Ghendon YuZ
D002725:Chloroform; D003588:Cytopathogenic Effect, Viral; D012321:DNA-Directed RNA Polymerases / Q000037:antagonists & inhibitors; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009980:Influenza A virus / Q000201:enzymology; D007370:Interferon Type I / Q000032:analysis* / Q000302:isolation & purification; D000432:Methanol; D011506:Proteins / Q000032:analysis / Q000302:isolation & purification* / Q000494:pharmacology; D012261:Ribonucleoproteins / Q000378:metabolism; D012995:Solubility
D007370:Interferon Type I; D011506:Proteins; D012261:Ribonucleoproteins; D002725:Chloroform; D012321:DNA-Directed RNA Polymerases; D000432:Methanol