pH dependent effect of glycosylation on protein stability.

pH dependent effect of glycosylation on protein stability. Research Abstract Details 

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pH dependent effect of glycosylation on protein stability. Abstract Text:

Wei Wang,Kris Antonsen,Y John Wang,D Q Wang,Wei Wang,Kris Antonsen,Y John Wang,D Q Wang,

The effect of glycosylation state on the thermal and storage stability of interleukin-2 mutein (IL-2 mutein) was investigated. The thermal stability of IL-2 mutein was studied by DSC and UV. An accelerated storage stability study was conducted at 40 degrees C in the dark and analyzed by UV, SDS-PAGE, and RP-HPLC. The unfolding temperatures (T(u)) of both glycosylated and unglycosylated forms of IL-2 mutein are similar (within +/-1 degrees C) at pH 5.5 and 7.5. At pH 4.0, the T(u) of glycosylated IL-2 mutein was 4 degrees C lower than that of the unglycosylated form. The precipitation temperature of glycosylated IL-2 mutein is similar to that of the unglycosylated form at pH 5.5 but 4 degrees C higher at pH 7.5. The precipitation temperature is not detectable for both forms at pH 4.0. During storage, both glycosylated and unglycosylated IL-2 mutein form aggregates (soluble and insoluble) and other degradation products. The aggregates are formed by both physical and chemical mechanisms. The major pathway of chemical aggregation appears to be disulfide bond formation/exchange. The glycosylated form is much less stable than the unglycosylated form at pH 4.0 and both forms are most stable at pH 5.5 in terms of thermal stability, precipitation rate and total degradation rate. This study clearly demonstrates that the effect of glycosylation on the stability of a protein is pH-dependent.

pH dependent effect of glycosylation on protein stability. Publishing Authors By Initials

W Wang,K Antonsen,YJ Wang,DQ Wang,W Wang,K Antonsen,YJ Wang,DQ Wang,

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pH dependent effect of glycosylation on protein stability. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: European journal of pharmaceutical sciences : offi

VOLUME: 33

Page Numbers: 120-7

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ISSN: 0928-0987

DAY: 19

MONTH: 11

YEAR: 2007

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LANGUAGE: eng

NlmUniqueID: 9317982

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Grant and Affiliation Information for pH dependent effect of glycosylation on protein stability.

AFFILIATION: Pfizer Inc., Global Biologics, 700 Chesterfield Parkway West, Chesterfield, MO 63017, USA.

Country: Netherlands

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MEDLINETA: Eur J Pharm Sci

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