Medizinische Universität Graz - Research portal
Selected Publication:
Pifat, G; Brnjas-Kraljevic, J; Jürgens, G; Herak-Kramberger, CM; Herak, JN.
Chemical modification of low-density lipoprotein enhances the number of binding sites for divalent cations.
Chem Phys Lipids. 1992; 63(3):159-167
Doi: 10.1016/0009-3084(92)90032-K
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- Co-authors Med Uni Graz
- Jürgens Günther
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- Abstract:
- The EPR technique with paramagnetic Mn(II) ions has been used to probe the negatively charged sites on the surface of modified low-density lipoprotein (LDL). LDL modified in five different ways exhibited increased binding capacity for divalent cations. Enhanced binding is caused by the increase in the number of 'strong' binding sites. The 'strong' sites have been identified to be the aspartic acid and/or glutamic acid carboxyl residues and the 'weak' sites are zwitter-ionic phospholipids. In native LDL the negative groups make 'bonds' with the positive lysyl residues, thus stabilizing the structure. Any deprotonation or modification of the lysine amino groups makes the LDL structure more loose and the amino acid carboxyl groups accessible to divalent cations.
- Find related publications in this database (using NLM MeSH Indexing)
- Acetylation -
- Binding Sites -
- Cations, Divalent - metabolism
- Electron Spin Resonance Spectroscopy - metabolism
- Humans - metabolism
- Lipoproteins, LDL - chemistry
- Malondialdehyde - pharmacology
- Manganese - metabolism
- Methylation - metabolism
- Neuraminidase - pharmacology
- Receptors, LDL - metabolism
- Reference Values - metabolism
- Trinitrobenzenesulfonic Acid - pharmacology
- Find related publications in this database (Keywords)
- Electron Paramagnetic Resonance (EPR)
- Low-Density Lipoprotein (LDL)
- Modification
- LDL
- Stabilization of Structure
- Mn(II) Binding