Osago H, Mishima K, Tsuchiya M, Tanigawa Y, Umeno T, Shimoyama M
Department of Biochemistry, Shimane Medical University, Izumo, Japan.
Biochem Biophys Res Commun. 1991 Oct 15;180(1):64-8. doi: 10.1016/s0006-291x(05)81255-0.
We investigated immunohistochemically the localization of p33, an endogenous substrate protein for an arginine-specific ADP-ribosyltransferase in chicken liver. Polymorphonuclear-pseudo-eosinophilic granulocytes (heterophils) in interlobular connective tissues of the liver were exclusively and strongly stained with the antibody against p33. Strong reactivity was associated with granules in cytoplasm of the heterophils. When the chicken liver nuclear fraction was washed, the transferase activity was released into the 600 x g supernatant fraction while a nuclear enzyme poly(ADP-ribose) synthetase was retained in the pellet fraction. These results indicate that p33 and probably also ADP-ribosyltransferase, found in the liver nuclear fraction [Tanigawa et al. (1984) J. Biol. Chem. 259, 2022-2029, Mishima et al. (1988) Eur. J. Biochem. 179, 267-273], originate from interlobular heterophils of the chicken liver.
我们采用免疫组织化学方法研究了鸡肝脏中精氨酸特异性ADP - 核糖基转移酶的内源性底物蛋白p33的定位。肝脏小叶间结缔组织中的多形核假嗜酸性粒细胞（异嗜性粒细胞）被抗p33抗体特异性地强烈染色。强反应性与异嗜性粒细胞胞质中的颗粒有关。当对鸡肝脏核组分进行洗涤时，转移酶活性释放到600×g上清组分中，而核酶聚（ADP - 核糖）合成酶保留在沉淀组分中。这些结果表明，在肝脏核组分中发现的p33以及可能还有ADP - 核糖基转移酶[谷川等人（1984年）《生物化学杂志》259卷，2022 - 2029页，三岛等人（1988年）《欧洲生物化学杂志》179卷，267 - 273页]源自鸡肝脏的小叶间异嗜性粒细胞。
