Four identical subunits in jack fruit seed agglutinin offer only two saccharide binding sites

FEBS Letters

Appukuttan, P.S.¹  Basu, Debkumar¹ 

[1] Neurøchemistry Division, Sree Chitra Tirunal Institute for Medical Sciences and Technology, Trivandrum 695011, India

关键词: Jack fruit seed agglutinin;    Half-of-the-sites binding;    Equilibrium dialysis;    Fluorescence quenching;    JSA;    jack fruit seed agglutinin;    PBS;    potassium phosphate buffer (20 mM;    pH 7.4) containing 150 mM Nacl;    MeUmb α-Gal;    4-methylumbelliferyl α-D-galactopyranoside;    PNP α-Gal;    p-nitrophenyl α-D-galactopyranoside;    Gn.HCl;    guanidine hydrochloride;   

DOI  :  10.1016/0014-5793(85)81097-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Gel filtration of jack fruit seed agglutinin in 6 M guanidine hydrochloride confirmed our earlier report that the native 39.5-kDa protein was a tetramer of identical noncovalently associated 10-kDa subunits. Binding studies by the fluorescence quenching method using 4-methylumbelliferyl α-D-galactoside as well as equilibrium dialysis using p-nitrophenyl α-D-galactoside indicated only two binding sites per tetramer. This behaviour resembles the half-of-the-sites reactivity in certain enzymes and is discussed in view of the small subunit size.

【 授权许可】

Unknown