Results 131 to 140 of about 149 (147)
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Adrenoleukodystrophy and beta-galactosidase deficiency: Patient and carrier
Journal of Neurology, 1986A patient with adrenoleukodystrophy and his mother, a carrier, showed an elevated ratio of very long-chain fatty acids to long-chain fatty acids and decreased beta-galactosidase activity. Other lysosomal enzyme activities were normal except for the borderline level of arylsulfatase-A activity.
Yoshigoro Kuroiwa+3 more
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Beta-galactosidase from Aureobasidium pullulans
Letters in Applied Microbiology, 1989Aureobasidium pullulans is a new source of enzyme beta-galactosidase with optimum activity at pH 6·8 and a temperature of 45°C. Lactose induced enzyme synthesis, but low constitutive levels of enzyme were seen with other sugars. Addition of Mn2+ and Ca2+ increased enzyme production and activity. Co2+ was a strong activator of enzyme activity.
Vinay Rale+2 more
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HEPATIC BETA GALACTOSIDASE AND FELINE GMI GANGLIOSIDOSIS
Neuropathology and Applied Neurobiology, 1981Barnes I.C., Kelly D.F., Pennock C.A. & Randell J.A.J. (1981) Neuropathology and Applied Neurobiology 7, 463–476Hepatic beta galactosidase and feline GMI gangliosidosisThis paper describes the clinical, morphological and biochemical features of three cats with a progressive neurological disorder. Clinical features were ataxia and progressive tremor.
D. F. Kelly+3 more
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Beta-galactosidase immobilization on chitosan microspheres
Journal of Biotechnology, 2007Application of solid-phase biocatalysts has become important during the last decades. Enzymes could be immobilized on various supports and by different methods. The properties of immobilized biocatalysts are influenced by the characteristics of enzyme, support material and the immobilization method.
Bíró, Emese+4 more
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Inactivation of .beta.-galactosidase by iodination of tyrosine-253
Biochemistry, 1982Beta-Galactosidase is rapidly inactivated by iodination catalyzed by lactoperoxidase but is not inactivated in the presence of the substrate analogue, isopropyl beta-D-thiogalactoside (IPTG). Enzyme activity is lost upon the incorporation of 1 mol of iodine per mol of monomer, without dissociation of the tetrameric structure.
Irving Zabin+2 more
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Creation of a Recombinant Bacteriophage to Express Beta-Galactosidase
2014Human illness caused by the consumption of food contaminated with pathogenic bacteria is a worldwide problem that requires new detection methods to solve. The use of reporter bacteriophage as a device for detection of food-borne pathogens provides a promising new method to distinguish contaminated food and therefore prevent humans from infection ...
Swedberg, Catherine, Talbott, Heather
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Permeabilization of Streptococcus thermophilus and the expression of beta-galactosidase
Enzyme and Microbial Technology, 1994Studies were carried out to determine the efficacy of several permeabilizing agents in inducing high-level expression of β-galactosidase in Streptococcus thermophilus. Sodium dodecyl sulfate, Triton X-100, sodium deoxycholate, and one commercial bile acid preparation were effective as membrane destabilizing agents allowing lactose influx and hydrolysis
George A. Somkuti, Dennis H. Steinberg
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Immobilization of beta‐galactosidase on metal‐chelate‐substituted gels
Biotechnology and Applied Biochemistry, 1994The use of copper, zinc, iron, nickel and calcium in three different chelating gels was investigated for preparing immobilized beta‐galactosidase. The chelated ligands [Cu(2+)‐iminodiacetate (IDA), Cu(2+)‐Tris(carboxymethyl)ethylenediamine (TED), Ni(2+)‐IDA and Fe(3+)‐IDA] absorbed the protein so strongly that it can be considered a true immobilization.
Beatriz M. Brena+2 more
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New England Journal of Medicine, 1969
Abstract Deficient activity of beta galactosidase was found in the skin of two siblings with Hunter's syndrome and their mother, a carrier of the sex-linked disorder.
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Abstract Deficient activity of beta galactosidase was found in the skin of two siblings with Hunter's syndrome and their mother, a carrier of the sex-linked disorder.
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Beta-Galactosidase of Shigella Sonnei
Nature, 1963Carla R. Clausen, Mitsuru Nakamura
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