書誌事項
- タイトル別名
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- Changes in isoelectric point of variant vitamin D-binding protein(GC) by oxidation of substituted cystein(SH group).
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This study was made to explore the cause of appearance of unusual variant bands of vitamin D-binding protein (group-specific component, GC). Both GC 1A2 and GC 1A3 have two main bands and two minor bands, and both variants were characterized by having cystein instead of arginine at the codon 429. The minor bands disappeared by keeping them at 37°C, or adding CuSO4 or DTT to them. The results indicated that the characteristic main bands of GC 1A2 and GC 1A3 are derived from the oxidation of cystein (SH group) which corresponds to cystein at the codon 429.
収録刊行物
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- 生物物理化学
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生物物理化学 39 (1), 25-29, 1995
日本電気泳動学会
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詳細情報 詳細情報について
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- CRID
- 1390282679179066368
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- NII論文ID
- 130003607034
- 80008092756
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- ISSN
- 13499785
- 00319082
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可