通过sn-1,2-二酰甘油对恶性疟原虫裂殖子表面抗原进行酰化作用。
Acylation of a Plasmodium falciparum merozoite surface antigen via sn-1,2-diacyl glycerol.
作者信息
Haldar K, Ferguson M A, Cross G A
出版信息
J Biol Chem. 1985 Apr 25;260(8):4969-74.
The 195-kDa merozoite protein synthesized in schizonts of Plasmodium falciparum (Holder, A. A., and Freeman, R. R. (1982) J. Exp. Med. 156, 1528-1538) contains ester-linked fatty acid. Enzymatic treatment of the purified acylated protein established that the lipid is present as sn-1,2-diacyl glycerol, most probably linked to a phosphodiester at the 3-position of glycerol. The phosphodiglyceride is not directly esterified to an amino acid residue on the polypeptide backbone. The 195-kDa protein is processed to three fragments (83, 42, and 19 kDa) on the surface of free merozoites (Holder, A. A., and Freeman, R. R. (1984) J. Exp. Med. 160, 624-629), of which only the 42-kDa polypeptide is acylated.
在恶性疟原虫裂殖体中合成的195-kDa裂殖子蛋白（Holder, A. A., and Freeman, R. R. (1982) J. Exp. Med. 156, 1528 - 1538）含有酯连接脂肪酸。对纯化的酰化蛋白进行酶处理表明，脂质以sn-1,2-二酰甘油的形式存在，很可能与甘油3位上的磷酸二酯相连。磷酸二甘油酯并不直接酯化到多肽主链上的氨基酸残基。195-kDa蛋白在游离裂殖子表面被加工成三个片段（83、42和19 kDa）（Holder, A. A., and Freeman, R. R. (1984) J. Exp. Med. 160, 624 - 629），其中只有42-kDa多肽被酰化。
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