期刊论文详细信息
FEBS Letters
Four identical subunits in jack fruit seed agglutinin offer only two saccharide binding sites
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.
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【 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   

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