Human apolipoprotein B: partial amino acid sequence

FEBS Letters

Shively, John E.³  Balla, Maria A.¹  Lusis, Aldons J.²  LeBoeuf, Renee C.¹  Schumaker, Verne N.¹  Miller, Chad³ 

[1] The Molecular Biology Institute, and the Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024, USA;Departments of Medicine and Microbiology, UCLA, Los Angeles, CA 90024, USA;Department of Immunology, City of Hope Hospital and Beckman Research Institute, Duarte, CA 91010, USA

关键词: Apolipoprotein B;    Amino acid sequence;    Proteolysis;    LDL;    Protein isolation;    Polypeptide composition;   

DOI  :  10.1016/0014-5793(84)81378-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown