Primary structure and comparative sequence-analysis of an insect apolipoprotein: apolipophorin-Iii from Manduca-sexta
作者： K D Cole , G P Fernando-Warnakulasuriya , M S Boguski , M Freeman , J I Gordon
DOI: 10.1016/S0021-9258(18)60882-8
关键词: Sequence analysis 、 Amino acid 、 Protein primary structure 、 Peptide sequence 、 Biochemistry 、 Protein sequencing 、 Apolipophorin III 、 Biology 、 Complementary DNA 、 Manduca sexta
摘要: The amino acid sequence of an insect apolipoprotein, apolipophorin-III from Manduca sexta, was determined by a combination cDNA and protein sequencing. mature hemolymph consists 166 acids. also encodes for amino-terminal extension 23 acids which is not represented in the protein. existence precursor confirmed vitro translation fat body mRNA. Computer-assisted comparative analysis revealed following points: 1) composed tandemly repeating tetradecapeptide units with high potential forming amphiphilic helical structures. Compared to mammalian apolipoproteins repeat apolipoprotein show considerable length variability; 2) has striking resemblance several human including apoE, AIV, AI, CI. However, homology seems be entirely functional since, although apoproteins contain very similar types residues, actual degree identity quite low. Whether are derived common ancestral helix forming, lipid-binding protein, or arose convergent evolution can at present. This represents first complete apolipoprotein.
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