A POSSIBLE CALCIUM-BINDING SITE IN ANIMAL LECTINS - A H-1-NMR STUDY OF THE INTERACTION BETWEEN LANTHANIDES AND A SYNTHETIC PEPTIDE FROM A HIGHLY CONSERVED DOMAIN OF PLEURODELES LECTIN

被引:5
作者
BONDON, A [1 ]
TIFFOCHE, C [1 ]
SIMONNEAUX, G [1 ]
LEPENNEC, JP [1 ]
JEGO, P [1 ]
机构
[1] UNIV RENNES 1, PHYSIOL REGULAT LAB, CNRS, URA 256, F-35042 RENNES, FRANCE
关键词
NMR; LANTHANIDE; METAL BINDING SITE;
D O I
10.1016/0167-4889(92)90161-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
H-1-NMR techniques have been used to study the metal binding properties of a synthetic peptide of 15 amino acids corresponding to a highly conserved domain of Pleurodeles lectin. The addition of lanthanum chloride or praseodymium chloride in a peptide solution induces some conformational changes as displayed by several concerted variations of peptide resonances. The Ln3+ concentration dependence of the chemical shifts was used to calculate the Ln3+ binding constants. The dissociation constants of 95-mu-M and 280-mu-M were found for La3+ and Pr3+, respectively.
引用
收藏
页码:19 / 26
页数:8
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