The solid phase synthesis of a protein activator for lecithin-cholesterol acyltransferase corresponding to human plasma apoC-I.
Apolipoprotein C-I, a protein constituent of the very low density lipoproteins of human plasma, consists of a single chain of 57 amino acids. The total synthesis of a protein corresponding to apolipoprotein C-I in physical properties and compositions was accomplished by solid phase techniques employing a modified polystrene incorporating spacer groups between the point of attachment of the first residue and the polymer matrix. The synthetic apoprotein was shown to activate lecithin:cholesterol acyltransferase to the same extent as the native protein. Comparative lipid-binding studies with dimyristoyl phosphatidylcholine gave complexes for native and synthetic apoprotein which floated at the same density after ultracentrifugation in KBr gradients and had virtually the same lipid:protein ratios.
D000217:Acyltransferases / Q000378:metabolism*; D001059:Apoproteins / Q000138:chemical synthesis* / Q000378:metabolism / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D008079:Lipoproteins, VLDL; D009226:Myristates; D007862:Phosphatidylcholine-Sterol O-Acyltransferase / Q000378:metabolism*; D010713:Phosphatidylcholines / Q000031:analogs & derivatives / Q000378:metabolism*; D011485:Protein Binding
D001059:Apoproteins; D008079:Lipoproteins, VLDL; D009226:Myristates; D010713:Phosphatidylcholines; D000217:Acyltransferases; D007862:Phosphatidylcholine-Sterol O-Acyltransferase