Olofsson S, Jeansson S, Lycke E
J Virol. 1981 May;38(2):564-70. doi: 10.1128/JVI.38.2.564-570.1981.
Lysates from herpes simplex virus type 1-infected cells were subjected to affinity chromatography on soybean and Helix pomatia lectins. One of the virus-specified glycoproteins, probably the herpes simplex virus type 1-specific gC glycoprotein, bound to the lectins and was eluted with N-acetylgalactosamine. The affinity chromatography permitted a high degree of purification of the type-specific glycoprotein with respect to both host cell components and other viral glycoproteins. The lectin affinity pattern of this glycoprotein indicates the presence of a terminal alpha-N-acetylgalactosamine in an oligosaccharide, a finding not reported previously for glycoproteins of enveloped viruses.
将单纯疱疹病毒1型感染细胞的裂解物在大豆凝集素和苹果蜗牛凝集素上进行亲和层析。一种病毒特异性糖蛋白，可能是单纯疱疹病毒1型特异性gC糖蛋白，与凝集素结合，并用N-乙酰半乳糖胺洗脱。亲和层析在宿主细胞成分和其他病毒糖蛋白方面都能对该型特异性糖蛋白进行高度纯化。这种糖蛋白的凝集素亲和模式表明在寡糖中存在末端α-N-乙酰半乳糖胺，这一发现以前未见有包膜病毒糖蛋白的报道。
