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

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13 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)96-102
Number of pages7
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Issue number1
Publication statusPublished - Jun 7 1996
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology


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