Isolation and characterization of sulfhydryl and disulfide peptides of human apolipoprotein B-100

C. Y. Yang, T. W. Kim, S. A. Weng, B. Lee, M. Yang, Antonio Gotto

Research output: Contribution to journalArticle

80 Scopus citations

Abstract

Twenty-three of the 25 cysteine residues in apolipoprotein B-100 have been isolated directly from tryptic or peptic peptide mixtures. Sixteen cysteine residues exist in disulfide forms: Cys-1-Cys-3, Cys-2-Cys-4, Cys-5-Cys-6, Cys-7-Cys-8, Cys-9-Cys-10, Cys-11-Cys-12, Cys-13-Cys-14, and Cys-20-Cys-21. All of these except Cys-20-Cys-21 are recently discovered disulfide linkages. In addition to Cys-22 and Cys-24, which have been described as sulfhydryls on low density lipoprotein, Cys-15 to Cys-18 and Cys-23 are in the reduced form. Cys-19 and Cys-25 are not yet confirmed. Our results revealed that all identified disulfide linkages are located in the trypsin-releasable regions and that all except Cys-1-Cys-3 and Cys-2-Cys-4 are linked to the neighboring cysteine. We propose a linear model of apolipoprotein B-100 in low density lipoprotein that wraps around the low density lipoprotein molecule.

Original languageEnglish (US)
Pages (from-to)5523-5527
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume87
Issue number14
DOIs
StatePublished - 1990

Keywords

  • Low density lipoprotein
  • Peptide purification
  • Protein structure

ASJC Scopus subject areas

  • Genetics
  • General

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