Adsorption of Succinylated Lysozyme on Hydroxyapatite

✍ Scribed by Allal Barroug; Jacques Fastrez; Jacques Lemaitre; Paul Rouxhet

• Publisher: Elsevier Science
• Year: 1997
• Tongue: English
• Weight: 135 KB
• Volume: 189
• Category: Article
• ISSN: 0021-9797
• DOI: 10.1006/jcis.1997.4787

✦ Synopsis

tories. Its chemical and textural characteristics have been Hen egg white lysozyme has been succinylated, the isoelectric reported before under the name HAP III (2); its surface area point being shifted thereby from about 11 to 4.5-4.7. Its adsorption is 80 m 2 rg 01 .

on a chromatography grade hydroxyapatite has been investigated

Hen egg white lysozyme (Sigma No. 6876, Grade 1) was at 20ЊC and in the pH range from 5.9 to 7.4. Adsorption takes succinylated following the method of Bernard et al. (3). A place despite an electrical repulsion between the surface and the large excess of succinic anhydride (mole fraction with readsorbate; consequently, it is favored by a decrease of pH and spect to the protein is about 360) was used in order to phosphate concentration and an increase of calcium concentration achieve a high degree of substitution. At room temperature and ionic strength. While adsorption of native lysozyme is driven (22 { 2)ЊC, 2 g of lysozyme were dissolved in 100 cm /3 by electrostatic attraction to the surface, adsorption of succinylated lysozyme is controlled by hydrophobic interactions. This may of a 50 mmolrdm 03 hepes buffer at pH 8.2 (Janssen Chimbe attributed to a different structure of modified lysozyme, comica) and NaCl was added to reach 1.25 molrdm 03 . After pared to native lysozyme, or to a greater tendency to undergo dissolution, 5 g of anhydrous succinic (Janssen Chimica) conformational changes.