Structure of apolipoprotein C-IIToronto, a nonfunctional human apolipoprotein.
We previously reported a family with apolipoprotein C-II (apoC-II) deficiency characterized by the presence of a mutant apoC-II, apoC-IIToronto. We now report the purification and primary structure of apoC-IIToronto. The sequence of apoC-IIToronto is identical to that of normal apoC-II from residues 1-68. It differs from residue 69, where Asp69-Gln70-Val71-Leu72-Ser73-Val74- Leu75-Lys76-Gly77-Glu78-Glu79 is replaced by Thr69-Lys70-Phe71-Phe72-Leu73-Cys74. This is consistent with the deletion of a nucleotide in the codon for either Thr68 or Asp69 and a translation reading frame shift.
Connelly
P W
PW
Maguire
G F
GF
Hofmann
T
T
Little
J A
JA
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D053304:Apolipoprotein C-II; D001056:Apolipoproteins C / Q000097:blood* / Q000302:isolation & purification; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D009154:Mutation; D010446:Peptide Fragments / Q000032:analysis
D000596:Amino Acids; D053304:Apolipoprotein C-II; D001056:Apolipoproteins C; D010446:Peptide Fragments; C050929:apolipoprotein C-II (Toronto)