| Autor: |
Sohei Ito, Tatsuda, Emi, Ishino, Kousuke, Suzuki, Kenichiro, Sakai, Hiroshi, Uchida, Koji |
| Předmět: |
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| Zdroj: |
Acta Crystallographica: Section F (Wiley-Blackwell); Jun2006, Vol. 62 Issue 6, p562-564, 3p, 1 Color Photograph, 1 Black and White Photograph, 1 Diagram, 1 Chart |
| Abstrakt: |
4-Hydroxy-2-nonenal (HNE), a major racemic product of lipid peroxidation, reacts with histidine to form a stable HNE–histidine Michael addition-type adduct possessing three chiral centres in the cyclic hemiacetal structure. Monoclonal antibodies against HNE-modified protein have been widely used for assessing oxidative stress in vitro and in vivo. Here, the purification, crystallization and preliminary crystallographic analysis of a Fab fragment of novel monoclonal antibody R310 (mAbR310), which recognizes ( R)-HNE-modified protein, are reported. The Fab fragment of mAbR310 was obtained by digestion with papain, purified and crystallized. Using hanging-drop vapour-diffusion crystallization techniques, crystals of mAbR310 Fab were obtained. The crystal belongs to the monoclinic space group C2 (unit-cell parameters a = 127.04, b = 65.31, c = 64.29 Å, β = 118.88°) and diffracted X-rays to a resolution of 1.84 Å. The asymmetric unit contains one molecule of mAbR310, with a corresponding crystal volume per protein weight of 2.51 Å3 Da−1 and a solvent content of 51.0%. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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