Phospholipase D Modified with a Polyethylene Glycol Derivative
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Phospholipase D from Streptomyces sp. AA586,PLDP, was modified with methoxypolyethylene glycol succinimidylsuccinate (ss-PEG), an active derivative of polyethylene glycol. By titration with trinitrobenzene sulfonate (TNBS), approximately 70% of the free amino groups in the enzyme protein were shown to be modified by treatment with ss-PEG. By this modification, the molecular weight of the enzyme was increased, judging from the results of sodium dodecyl sulfate-polyacrylamide gel electrophoresis, gel filtration with Toyopearl HW-55F and TNBS titration. Due to the loss of cationic charges, the enzyme protein became eluted faster in high performance liquid chromatography with CM-Toyopearl. By modification with ss-PEG, the enzyme became fairly thermostable, while pH-stability and optimal pH were not influenced. The value of K_m for phosphatidylcholine of the hydrolytic reaction increased 2-fold, whereas that of the transphosphatidyl reaction was not significantly altered.
収録刊行物
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- Chemical & pharmaceutical bulletin
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Chemical & pharmaceutical bulletin 39 (3), 743-746, 1991-03-25
公益社団法人日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1573950402227454720
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- NII論文ID
- 110003629199
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- NII書誌ID
- AA00602100
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- ISSN
- 00092363
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- 本文言語コード
- en
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- データソース種別
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- CiNii Articles