Ovalbumin in developing chicken eggs migrates from egg white to embryonic organs while changing its conformation and thermal stability

Yasushi Sugimoto, Shinya Sanuki, Seiichiroh Ohsako, Yuichiro Higashimoto, Michio Kondo, Junichi Kurawaki, Hisham R. Ibrahim, Takayoshi Aoki, Takahiro Kusakabe, Katsumi Koga

研究成果: Contribution to journalArticle

74 被引用数 (Scopus)

抄録

Ovalbumin was detected in developing chicken eggs. The large majority of these ovalbumin molecules was found to be in a heat-stable form reminiscent of S-ovalbumin. About 83 and 90% of the ovalbumin population was in a heat- stable form in day 14 or stage 40 amniotic fluid and day 18 or stage 44 egg yolk, respectively, whereas ovalbumin in newly deposited eggs was in the heat-unstable, native form. Purified preparations of stable ovalbumin from egg white and amniotic fluid showed a less ordered configuration than native ovalbumin, as analyzed by circular dichroism and differential scanning calorimetry. In addition, mass spectrometric analysis exhibited distinct size microheterogeneity between the stable and native forms of ovalbumin. Immunohistochemical study revealed that ovalbumin was present in the central nervous system and other embryonic organs. These results indicated that egg white ovalbumin migrates into the developing embryo while changing its higher order structure.

本文言語英語
ページ(範囲)11030-11037
ページ数8
ジャーナルJournal of Biological Chemistry
274
16
DOI
出版ステータス出版済み - 4 16 1999

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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