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gONC increases conformational stability and toxicity for cancer cells.

Vaccine Weekly

| May 05, 2004 | COPYRIGHT 2004 NewsRX. This material is published under license from the publisher through the Gale Group, Farmington Hills, Michigan.  All inquiries regarding rights should be directed to the Gale Group. (Hide copyright information)Copyright

2004 MAY 5 - (NewsRx.com & NewsRx.net) -- Glycosylation of onconase increases its conformational stability and toxicity for cancer cells.

"Onconase (ONC) is currently in Phase III clinical trials as a cancer chemotherapeutic agent. Despite the finding that ONC contains an N-linked glycosylation site (-N69-V70-T71-), only the non-glycosylated form of the protein has been identified to date." The Pichia pastoris expression system was employed "to produce recombinant glycosylated ONC (gONC)protein," wrote scientists in South Korea.

"Approximately 10 mg of ONC protein was secreted per liter of culture media, of which about 80% was glycosylated at N69. CD spectroscopic analyses revealed that the secondary structure of gONC is identical to that of ONC." gONC was determined to contain "a high-mannose core structure. Importantly, glycosylation of ONC at N69 greatly increased its toxicity for K-562 cancer cells. Specifically, the IC[subscript]50 value of gONC was 50-fold lower than that of ONC," reported B.M. Kim and colleagues.

"Glycosylation increased both the T-m of ONC and ...

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Source: HighBeam Research, gONC increases conformational stability and toxicity for cancer cells.

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