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一种从金针菇中分离得到的新型真菌免疫调节蛋白FIP-fve及其完整氨基酸序列。

A new fungal immunomodulatory protein, FIP-fve isolated from the edible mushroom, Flammulina velutipes and its complete amino acid sequence.

作者信息

Ko J L, Hsu C I, Lin R H, Kao C L, Lin J Y

机构信息

Institute of Biochemistry, College of Medicine, National Taiwan University, Taipei, Republic of China.

出版信息

Eur J Biochem. 1995 Mar 1;228(2):244-9.

PMID:7705335
Abstract

A new fungal immunomodulatory protein (FIP-fve) has been isolated and purified from the edible golden needle mushroom (Flammulina velutipes). The apparent molecular mass of FIP-fve determined by SDS/PAGE agrees well with the value of 12704 Da calculated from its amino acid composition and sequence. The complete amino acid sequence of FIP-fve was elucidated by protein sequencing techniques. FIP-fve consists of 114 amino acid residues with an acetylated amino end, and lacks methionine, half-cystine and histidine residues. FIP-fve was able to hemagglutinate human red blood cells. The immunomodulatory activity of FIP-fve was demonstrated by its stimulatory activity toward human peripheral blood lymphocytes, and its suppression of systemic anaphylaxis reactions and local swelling of mouse footpads. FIP-fve was found to enhance the transcriptional expression of interleukin-2 and interferon-gamma.

摘要

一种新的真菌免疫调节蛋白(FIP-fve)已从可食用的金针菇(Flammulina velutipes)中分离纯化出来。通过SDS/PAGE测定的FIP-fve的表观分子量与根据其氨基酸组成和序列计算出的12704 Da的值非常吻合。FIP-fve的完整氨基酸序列通过蛋白质测序技术得以阐明。FIP-fve由114个氨基酸残基组成,氨基末端乙酰化,并且缺乏甲硫氨酸、半胱氨酸和组氨酸残基。FIP-fve能够凝集人红细胞。FIP-fve的免疫调节活性通过其对人外周血淋巴细胞的刺激活性以及对小鼠全身过敏反应和足垫局部肿胀的抑制作用得以证明。发现FIP-fve可增强白细胞介素-2和干扰素-γ的转录表达。

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