Albrechtsen M, Yeaman G R, Kerr M A
Department of Pathology, University of Dundee, Ninewells Hospital and Medical School, U.K.
Immunology. 1988 Jun;64(2):201-5.
Human polymorphonuclear leucocytes (PMNs) will phagocytose yeasts opsonized with specific affinity-purified human serum IgA. PMNs also bind to Sepharose beads coated with IgA or IgG, but not to beads coated with bovine serum albumin (BSA) or horseradish peroxidase (HRP). Binding to IgA-Sepharose stimulates the cells to release lysozyme. Affinity chromatography of 125I-labelled PMN membrane proteins on IgA-Sepharose results in isolation of a polypeptide of apparent 60,000 MW. The protein, which is not bound to IgG-Sepharose under the same conditions, appears as a diffuse band on SDS-PAGE, suggesting it is heavily glycosylated.
人类多形核白细胞（PMNs）会吞噬经特异性亲和纯化的人血清IgA调理的酵母。PMNs也会与包被有IgA或IgG的琼脂糖珠结合，但不会与包被有牛血清白蛋白（BSA）或辣根过氧化物酶（HRP）的珠子结合。与IgA-琼脂糖珠的结合会刺激细胞释放溶菌酶。用IgA-琼脂糖对125I标记的PMN膜蛋白进行亲和层析，可分离出一种表观分子量为60,000的多肽。在相同条件下，该蛋白不与IgG-琼脂糖珠结合，在SDS-PAGE上呈现为一条弥散带，表明它高度糖基化。
