A proteinase inhibitor from egg yolk of hen is an ovoinhibitor analog

Yasushi Sugimoto, Takahiro Kusakabe, Sumiharu Nagaoka, Takashi Nirasawa, Kazue Tatsuguchi, Makoto Fujii, Takayoshi Aoki, Katsumi Koga

研究成果: ジャーナルへの寄稿記事

12 引用 (Scopus)

抄録

A proteinase inhibitor, tentatively termed vitelloinhibitor, was purified from yolk of hen's ovarian follicles. It resembled egg-white ovoinhibitor not only in inhibitory spectrum (active for bovine trypsin and bovine chymotrypsin) but also in thermal stability, pH stability, antiserum reactivity and amino-acid composition. However, vitelloinhibitor had different molecular weight from that of ovoinhibitor. An α2-proteinase inhibitor preparation, isolated from laying hen's serum in the present study, was found to exhibit two bands, and the larger one of the latter corresponded to vitelloinhibitor in molecular weight. The partial N-terminal amino-acid sequence of vitelloinhibitor was the same as those of the two components of serum inhibitor and all three agreed with that of ovoinhibitor. Vitelloinhibitor is likely to be an ovoinhibitor analog derived from a serum precursor, which might be the larger component of α2-proteinase inhibitor.

元の言語英語
ページ(範囲)96-102
ページ数7
ジャーナルBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
1295
発行部数1
DOI
出版物ステータス出版済み - 6 7 1996

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Egg Yolk
Peptide Hydrolases
Molecular Weight
Serum
Molecular weight
Amino Acids
Egg White
Ovarian Follicle
Chymotrypsin
Trypsin
Immune Sera
Amino Acid Sequence
Thermodynamic stability
Hot Temperature
ovoinhibitor
Chemical analysis

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

これを引用

A proteinase inhibitor from egg yolk of hen is an ovoinhibitor analog. / Sugimoto, Yasushi; Kusakabe, Takahiro; Nagaoka, Sumiharu; Nirasawa, Takashi; Tatsuguchi, Kazue; Fujii, Makoto; Aoki, Takayoshi; Koga, Katsumi.

:: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 巻 1295, 番号 1, 07.06.1996, p. 96-102.

研究成果: ジャーナルへの寄稿記事

Sugimoto, Yasushi ; Kusakabe, Takahiro ; Nagaoka, Sumiharu ; Nirasawa, Takashi ; Tatsuguchi, Kazue ; Fujii, Makoto ; Aoki, Takayoshi ; Koga, Katsumi. / A proteinase inhibitor from egg yolk of hen is an ovoinhibitor analog. :: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology. 1996 ; 巻 1295, 番号 1. pp. 96-102.
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abstract = "A proteinase inhibitor, tentatively termed vitelloinhibitor, was purified from yolk of hen's ovarian follicles. It resembled egg-white ovoinhibitor not only in inhibitory spectrum (active for bovine trypsin and bovine chymotrypsin) but also in thermal stability, pH stability, antiserum reactivity and amino-acid composition. However, vitelloinhibitor had different molecular weight from that of ovoinhibitor. An α2-proteinase inhibitor preparation, isolated from laying hen's serum in the present study, was found to exhibit two bands, and the larger one of the latter corresponded to vitelloinhibitor in molecular weight. The partial N-terminal amino-acid sequence of vitelloinhibitor was the same as those of the two components of serum inhibitor and all three agreed with that of ovoinhibitor. Vitelloinhibitor is likely to be an ovoinhibitor analog derived from a serum precursor, which might be the larger component of α2-proteinase inhibitor.",
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AU - Nagaoka, Sumiharu

AU - Nirasawa, Takashi

AU - Tatsuguchi, Kazue

AU - Fujii, Makoto

AU - Aoki, Takayoshi

AU - Koga, Katsumi

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N2 - A proteinase inhibitor, tentatively termed vitelloinhibitor, was purified from yolk of hen's ovarian follicles. It resembled egg-white ovoinhibitor not only in inhibitory spectrum (active for bovine trypsin and bovine chymotrypsin) but also in thermal stability, pH stability, antiserum reactivity and amino-acid composition. However, vitelloinhibitor had different molecular weight from that of ovoinhibitor. An α2-proteinase inhibitor preparation, isolated from laying hen's serum in the present study, was found to exhibit two bands, and the larger one of the latter corresponded to vitelloinhibitor in molecular weight. The partial N-terminal amino-acid sequence of vitelloinhibitor was the same as those of the two components of serum inhibitor and all three agreed with that of ovoinhibitor. Vitelloinhibitor is likely to be an ovoinhibitor analog derived from a serum precursor, which might be the larger component of α2-proteinase inhibitor.

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