Abstract
Using the fluorescent sulfhydryl probe, 5-iodoacetamidofluoresceine, to label the free sulfhydryl of low-density lipoprotein, the positions of two cysteine residues in apolipoprotein B were located. The tryptic peptides containing the fluorescent probe were isolated by high-performance liquid chromatography systems and sequenced by automatic techniques. The free cysteine residues of apolipoprotein B-100 on low-density lipoprotein are located at positions 3734 and 4190, either or both of which can potentially form a disulfide linkage with apolipoprotein(a) in lipoprotein(a).
Original language | English (US) |
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Pages (from-to) | 129-132 |
Number of pages | 4 |
Journal | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular |
Volume | 1037 |
Issue number | 1 |
DOIs | |
State | Published - Jan 19 1990 |
Keywords
- Amino acid sequence
- Apolipoprotein B-100
- Fluorescent labeling
- Lipoprotein (a)
- Low density lipoproteins
- Sulfhydryl peptide
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
- Biophysics
- Biochemistry