TY - JOUR
T1 - Acylation of a Plasmodium falciparum merozoite surface antigen via sn-1,2-diacyl glycerol
AU - Haldar, Kasturi
AU - Ferguson, Michael A. J.
AU - Cross, George A. M.
PY - 1985/4/25
Y1 - 1985/4/25
N2 - 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 aid. 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.
AB - 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 aid. 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.
UR - http://www.scopus.com/inward/record.url?scp=0021860850&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0021860850
SN - 0021-9258
VL - 260
SP - 4969
EP - 4974
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 8
ER -