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

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1135卷 / 01期

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

页码：19 / 26

页数：8

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