She Q B, Ng T B, Liu W K
Department of Anatomy, Faculty of Medicine, Chinese University of Hong Kong, Shatin, N. T.
Biochem Biophys Res Commun. 1998 Jun 9;247(1):106-11. doi: 10.1006/bbrc.1998.8744.
A novel lectin has been purified from the fruiting bodies as well as cultured mycelia of the edible mushroom Volvariella volvacea. The lectin, designated as VVL, was a homodimeric protein with a molecular weight of 32 kDa as demonstrated by gel filtration and SDS-PAGE. VVL had no carbohydrate moiety, and its hemagglutinating activity was inhibited by thyroglobulin but not by simple carbohydrates such as monomeric or dimeric sugars. The immunomodulatory activity of VVL was demonstrated by its potent stimulatory activity toward murine splenic lymphocytes. VVL was also found to markedly enhance the transcriptional expression of interleukin-2 and interferon-gamma by reverse transcriptase-polymerase chain reaction. As revealed by its N-terminal amino acid sequence, VVL possessed a molecular structure distinct from other immunomodulatory proteins previously reported in the same fungus.
一种新型凝集素已从草菇的子实体以及培养的菌丝体中纯化出来。这种凝集素被命名为VVL,通过凝胶过滤和SDS-PAGE证明它是一种分子量为32 kDa的同二聚体蛋白。VVL没有碳水化合物部分,其血凝活性受到甲状腺球蛋白的抑制,但不受单糖或二糖等简单碳水化合物的抑制。VVL对小鼠脾淋巴细胞具有强大的刺激活性,从而证明了其免疫调节活性。通过逆转录聚合酶链反应还发现VVL能显著增强白细胞介素-2和干扰素-γ的转录表达。从其N端氨基酸序列可知,VVL具有与先前在同一真菌中报道的其他免疫调节蛋白不同的分子结构。