TY - JOUR
T1 - Characterization of a nonspecific activator protein for the enzyme hydrolysis of glycolipids
AU - Li, S. C.
AU - Sonnino, S.
AU - Tettamanti, G.
AU - Li, Y. T.
PY - 1988
Y1 - 1988
N2 - We have studied the substrate specificities of a non-specific activator protein on the enzymatic hydrolyses of the following compounds: G(M1) and G(M2), as well as several of their derivatives including oligosaccharides, GgOse3Cer-II3-sulfate and LacCer-II3-sulfate, Gb-Ose3Cer and GgOse4Cer, three neolacto-series glycosphingolipids, and two non-ceramide glycolipids. Our results show that this activator protein has a broad spectrum of activity and exhibits the properties of a nonspecific natural detergent. The evidence of non-specificity was the ability of this activator protein to stimulate the hydrolyses of glycolipids, regardless of glycosphingolipids or non-ceramide glycolipids, carried out by glycosidases from animals, plants, and microorganisms. Its activity was, however, limited to substrates that had a lipid moiety. The oligosaccharide of G(M1) and deacetyl-fatty acid free G(M1) (II3-NeuGg-Ose4-sphingosine) were hydrolyzed by β-galactosidase in the absence of this activator protein.
AB - We have studied the substrate specificities of a non-specific activator protein on the enzymatic hydrolyses of the following compounds: G(M1) and G(M2), as well as several of their derivatives including oligosaccharides, GgOse3Cer-II3-sulfate and LacCer-II3-sulfate, Gb-Ose3Cer and GgOse4Cer, three neolacto-series glycosphingolipids, and two non-ceramide glycolipids. Our results show that this activator protein has a broad spectrum of activity and exhibits the properties of a nonspecific natural detergent. The evidence of non-specificity was the ability of this activator protein to stimulate the hydrolyses of glycolipids, regardless of glycosphingolipids or non-ceramide glycolipids, carried out by glycosidases from animals, plants, and microorganisms. Its activity was, however, limited to substrates that had a lipid moiety. The oligosaccharide of G(M1) and deacetyl-fatty acid free G(M1) (II3-NeuGg-Ose4-sphingosine) were hydrolyzed by β-galactosidase in the absence of this activator protein.
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M3 - Article
C2 - 3360793
AN - SCOPUS:0023919106
VL - 263
SP - 6588
EP - 6591
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 14
ER -