TY - JOUR
T1 - A proteinase inhibitor from egg yolk of hen is an ovoinhibitor analog
AU - Sugimoto, Yasushi
AU - Kusakabe, Takahiro
AU - Nagaoka, Sumiharu
AU - Nirasawa, Takashi
AU - Tatsuguchi, Kazue
AU - Fujii, Makoto
AU - Aoki, Takayoshi
AU - Koga, Katsumi
N1 - Funding Information:
We wish to express a thank to Mrs. H. Yatsuki of Saga Medical School for her excellent assistance. This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan, and in part by a Science Research Promotion Fund from the Japan Private School Promotion Foundation.
PY - 1996/6/7
Y1 - 1996/6/7
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.
AB - 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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U2 - 10.1016/0167-4838(96)00034-9
DO - 10.1016/0167-4838(96)00034-9
M3 - Article
C2 - 8679679
AN - SCOPUS:0005613279
SN - 0167-4838
VL - 1295
SP - 96
EP - 102
JO - Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
JF - Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
IS - 1
ER -