人α1-酸性糖蛋白（血清类黏蛋白）的白细胞表面起源
Leukocyte surface origin of human alpha1-acid glycoprotein (orosomucoid).
作者信息
Gahmberg C G, Andersson L C
出版信息
J Exp Med. 1978 Aug 1;148(2):507-21. doi: 10.1084/jem.148.2.507.
Abstract
Specific antibodies against human alpha1-acid glycoprotein reacted with human lymphocytes, granulocytes, and monocytes. The antigen on the leukocytes is an externally located integral membrane glycoprotein which is made by the cells and has an apparent mol wt of 52,000. It is released from cells in vitro to the culture medium. The mol wt of the soluble fragment is 41,000, which corresponds to that of alpha1-acid glycoprotein in serum and urine. Peptide mapping confirmed that the main part of the cellular membrane antigen consists of alpha1-acid glycoprotein with an additional, probably hydrophobic fragment. This finding may partially explain the increase in the serum levels of alpha1-acid glycoprotein observed in many disorders involving leukocyte proliferation. In addition, the known sequence homology of alpha1-acid glycoprotein with immunoglobulins can now be more easily understood by their origin in similar cell types.
摘要
抗人α1-酸性糖蛋白的特异性抗体可与人淋巴细胞、粒细胞和单核细胞发生反应。白细胞上的抗原是一种位于细胞外的整合膜糖蛋白，由细胞产生，表观分子量为52,000。它在体外从细胞释放到培养基中。可溶性片段的分子量为41,000，与血清和尿液中的α1-酸性糖蛋白分子量相当。肽图谱分析证实，细胞膜抗原的主要部分由α1-酸性糖蛋白组成，并带有一个额外的、可能是疏水的片段。这一发现可能部分解释了在许多涉及白细胞增殖的疾病中观察到的血清α1-酸性糖蛋白水平升高的现象。此外，鉴于α1-酸性糖蛋白与免疫球蛋白在相似细胞类型中的起源，现在可以更容易理解它们已知的序列同源性。
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