The primary structure of human plasma high density apolipoprotein glutamine I (ApoA-I). I. The amino acid sequence of cyanogen bromide fragment II.
Apolipoprotein glutamine I (apoLP-Gln-I or apoA-I) is one of the major protein constituents of human plasma high density lipoproteins. The protein has 245 amino acid residues, including 3 residues of methionine, and is lacking isoleucine, cystine, and cysteine. Cleavage of apoLP-Gln-I with cyanogen bromide yields four fragments, designated in their order of elution from Bio-Gel P-30 as CNBr I, II, III, and IV. In the present study, we report the complete amino acid sequence of the NH2-terminal fragment, CNBr II, a peptide that contains 90 amino acid residues.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001059:Apoproteins / Q000097:blood; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D005973:Glutamine / Q000032:analysis; D006801:Humans; D008075:Lipoproteins, HDL / Q000097:blood; D010446:Peptide Fragments / Q000032:analysis; D013820:Thermolysin; D014357:Trypsin
D000596:Amino Acids; D001059:Apoproteins; D008075:Lipoproteins, HDL; D010446:Peptide Fragments; D005973:Glutamine; D002918:Chymotrypsin; D014357:Trypsin; D013820:Thermolysin; D003488:Cyanogen Bromide