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: ジャーナルへの寄稿記事

71 引用 (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.

元の言語英語
ページ(範囲)11030-11037
ページ数8
ジャーナルJournal of Biological Chemistry
274
発行部数16
DOI
出版物ステータス出版済み - 4 16 1999

Fingerprint

Egg White
Ovalbumin
Eggs
Conformations
Chickens
Thermodynamic stability
Hot Temperature
Amniotic Fluid
Egg Yolk
Fluids
Differential Scanning Calorimetry
Neurology
Circular Dichroism
Differential scanning calorimetry
Embryonic Structures
Central Nervous System
Molecules

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Ovalbumin in developing chicken eggs migrates from egg white to embryonic organs while changing its conformation and thermal stability. / Sugimoto, Yasushi; Sanuki, Shinya; Ohsako, Seiichiroh; Higashimoto, Yuichiro; Kondo, Michio; Kurawaki, Junichi; Ibrahim, Hisham R.; Aoki, Takayoshi; Kusakabe, Takahiro; Koga, Katsumi.

:: Journal of Biological Chemistry, 巻 274, 番号 16, 16.04.1999, p. 11030-11037.

研究成果: ジャーナルへの寄稿記事

Sugimoto, Y, Sanuki, S, Ohsako, S, Higashimoto, Y, Kondo, M, Kurawaki, J, Ibrahim, HR, Aoki, T, Kusakabe, T & Koga, K 1999, 'Ovalbumin in developing chicken eggs migrates from egg white to embryonic organs while changing its conformation and thermal stability', Journal of Biological Chemistry, 巻. 274, 番号 16, pp. 11030-11037. https://doi.org/10.1074/jbc.274.16.11030
Sugimoto, Yasushi ; Sanuki, Shinya ; Ohsako, Seiichiroh ; Higashimoto, Yuichiro ; Kondo, Michio ; Kurawaki, Junichi ; Ibrahim, Hisham R. ; Aoki, Takayoshi ; Kusakabe, Takahiro ; Koga, Katsumi. / Ovalbumin in developing chicken eggs migrates from egg white to embryonic organs while changing its conformation and thermal stability. :: Journal of Biological Chemistry. 1999 ; 巻 274, 番号 16. pp. 11030-11037.
@article{078b19d71a974fedad948686aee22027,
title = "Ovalbumin in developing chicken eggs migrates from egg white to embryonic organs while changing its conformation and thermal stability",
abstract = "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.",
author = "Yasushi Sugimoto and Shinya Sanuki and Seiichiroh Ohsako and Yuichiro Higashimoto and Michio Kondo and Junichi Kurawaki and Ibrahim, {Hisham R.} and Takayoshi Aoki and Takahiro Kusakabe and Katsumi Koga",
year = "1999",
month = "4",
day = "16",
doi = "10.1074/jbc.274.16.11030",
language = "English",
volume = "274",
pages = "11030--11037",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "16",

}

TY - JOUR

T1 - Ovalbumin in developing chicken eggs migrates from egg white to embryonic organs while changing its conformation and thermal stability

AU - Sugimoto, Yasushi

AU - Sanuki, Shinya

AU - Ohsako, Seiichiroh

AU - Higashimoto, Yuichiro

AU - Kondo, Michio

AU - Kurawaki, Junichi

AU - Ibrahim, Hisham R.

AU - Aoki, Takayoshi

AU - Kusakabe, Takahiro

AU - Koga, Katsumi

PY - 1999/4/16

Y1 - 1999/4/16

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0033574609&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033574609&partnerID=8YFLogxK

U2 - 10.1074/jbc.274.16.11030

DO - 10.1074/jbc.274.16.11030

M3 - Article

C2 - 10196185

AN - SCOPUS:0033574609

VL - 274

SP - 11030

EP - 11037

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 16

ER -