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Separation and properties of α-galactosidase and β-galactosidase from Cajanus indicus

Biochimica et Biophysica Acta (BBA) - Enzymology, 1974
Abstract Cajanus indicus α- and β-galactosidase which are inseparable by Sephadex gel-chromatography (Dey, P. M. (1973) Biochim. Biophys. Acta 302, 393–398), have now been separated by CM-cellulose chromatography. α-Galactosidase (EC 3.2.1.22) has been resolved into two isoenzymes and β-galactosidase (EC 3.2.1.23) into three.
M. Dixon, Prakash M. Dey
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α-Galactosidase A in Vascular Disease

Trends in Cardiovascular Medicine, 2007
Deficiency of alpha-galactosidase A (GLA) (Fabry disease) leads to the accumulation of glycosphingolipids in the vasculature leading to multiorgan pathology. In addition to well-described microvascular disease, deficiency of GLA is also characterized by premature macrovascular events such as stroke and possibly myocardial infarction.
James A. Shayman   +2 more
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Inhibition of glucosidases and galactosidases by polyols

Archives of Biochemistry and Biophysics, 1966
Abstract The hydrolyses of p-nitrophenyl α- and β-galactosides and p-nitrophenyl α- and β-glucosides by an α-galactosidase from Aspergillus fumigatis, an α-glucosidase from germinated barley, and almond β-glucosidase, which also has β-galactosidase activity, have been examined in the presence of glycerol, erythritol, d -threitol, ribitol, xylitol ...
Marianne V. Kelemen, W. J. Whelan
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On the mechanism of β-galactosidase induction

Archives of Biochemistry and Biophysics, 1961
Abstract A 30-sec. pulse of tritiated leucine was given to logarithmically growing cells of Escherichia coli during induction with either melibiose or galactose. β-Galactosidase was thereafter isolated, and its specific radioactivity compared to that of the average cellular protein.
Barbara E. Wright, Gregory McNeil
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Properties of mouse α-galactosidase

Biochimica et Biophysica Acta (BBA) - General Subjects, 1976
alpha-Galactosidase has been examined in various murine tissues using the substrate 4-methylumbelliferyl-alpha-galactoside. Mouse liver appears to contain a single major form of the enzyme, as judged by chromatography and electrophoresis. The enzmye was purified 467-fold with a yield of about 40% by a method involving chromatography on Concanavalin A ...
Lusis, A J, Paigen, K
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Endo‐β‐Galactosidases and Keratanase

Current Protocols in Molecular Biology, 1995
AbstractThis overview covers the endo‐β‐galactosidases; enzyme is capable of hydrolyzing a wide range of glycoconjugates. Endo‐β‐galactosidases from numerous sources are discussed in terms of their substrate specificities and substrates, as well as their practical research applications.
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Inhibition of cyclodextrins on α-galactosidase

Food Chemistry, 2017
This work successfully investigated the effects of different influential factors and hydrophobic cavities of cyclodextrins (CDs) on α-galactosidase (α-Gal) by detecting α-Gal activity. The highest inhibitory concentration of three kinds of CDs (α-, β-, and γ-CD) on α-Gal was 10mM.
Ding Wenping   +15 more
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Dissociation of β-Galactosidase by Thiols

Nature, 1970
IT is common practice to add mercaptoethanol to solutions of β-galactosidase during purification from Escherichia coli and to the stock solutions of the enzyme during storage. Although Craven et al.1 had reported that mercaptoethanol stabilizes the enzyme isolated from the K12 strain against thermal inactivation, Reithel and his coworkers2 observed ...
Barbara J. Grochowski   +2 more
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β-Galactosidases

2017
β-Galactosidase is one of the most important enzymes used in food processing and has nutritional, technological, and environmental applications. This chapter discusses the various microbial sources of this attention-grabbing enzyme. The characteristics of purified β-galactosidase in view of its applications in lactose hydrolysis and transglycosylation ...
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α-Galactosidases

2017
α-Galactosidase, or melibiase, is a highly versatile enzyme having diverse nutraceutical, pharmaceutical, and industrial applications. There are various galactosides that form substrates for this enzyme. This chapter lists the various microbial sources of α-galactosidase and the choice of fermentation technologies widely used for its production.
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