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Human apolipoprotein B: partial amino acid sequence
Author(s) -
LeBoeuf Renee C.,
Miller Chad,
Shively John E.,
Schumaker Verne N.,
Balla Maria A.,
Lusis Aldons J.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81378-2
Subject(s) - apolipoprotein b , sequence (biology) , peptide sequence , chemistry , biochemistry , gene , cholesterol
A successful approach has been developed for the sequencing of apolipoprotein B based upon the procedure of Cleveland et al. [(1977) J. Biol. Chem. 252, 1102–1106] involving limited proteolysis in the presence of sodium dodecyl sulfate. Staphylococcus aureus protease was employed to produce large peptides which were isolated in relatively pure form by preparative gel electrophoresis. Two peptides were partially sequenced using spinning‐cup microsequencing techniques. The sequences are: Peptide R2‐5, ‐Ala ‐ Leu ‐ Val ‐ Gly ‐ Ile ‐ Asn ‐ Gly ‐ Glu ‐ Ala ‐ Asn ‐ Leu ‐ Asp ‐ Phe ‐ Leu ‐ Asn ‐ Ile ‐ Pro ‐ Leu ‐ Arg‐ Ile ‐ Pro‐ Pro‐Met‐Arg‐(Arg)‐; and Peptide R3‐1, ‐Leu‐Val‐Ala‐Lys‐Pro‐Ser‐Val‐Ser‐Val‐Glu‐Phe‐Val‐Thr ‐Asn‐Met‐Gly‐Ile‐Ile‐Ile‐Pro‐Lys‐Phe‐Ala‐Arg‐. Several stretches of residues suitable for the construction of oligonucleotide probes have been identified.