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인간 Annexin Ⅰ의 구조와 Phospholipase A2와의 상호작용에 대한 Spectroscopy 연구
이봉진,이연희,방근수,이태우,김종국,김양배,나도선 ( Bong Jin Lee,Yeon Hee Lee,Keun Su Bang,Tae Woo Lee,Chong Kook Kim,Yang Bae Kim,Doe Sun Na ) 생화학분자생물학회 1994 BMB Reports Vol.27 No.2
Annexin I is a member of the annexin family of calcium dependent phospholipid binding proteins and is an in vitro phospholipase A2 (PLA₂) inhibitor. The mechanism of PLA₂ inhibition by annexin I is still ambiguous. The structure of annexin I was studied at the atomic, molecular level by using nuclear magnetic resonance (NMR), circular dichroism (CD) and fluorescence spectroscopy. Recombinant human annexin I and N-terminally truncated annexin I (1-31 deleted : d-annexin I) were purified and their NMR spectra were compared. The NMR spectra of the two were similar. When Ca^(2+) ion was added to annexin 1 and d-annexin I, peak broadening occurred,- but no significant spectroscopic change was observed. When porcine pancreatic PLA₂ was added to deuterium labeled annexin I, interaction of annexin 1 with PLA₂ was observed as indicated by the disappearnnce and shift of several peaks in the NMR spectra. This result supports a protein-protein interaction mechanism for PLA₂ inhibition by annexin I.