Studies on glucosaminidase. 2. Substrates for <i>N</i>-acetyl-β-glucosaminidase

Borooah, J.; Leaback, David H.; Walker, P. G.

doi:10.1042/bj0780106

Cited by 96 publications

(32 citation statements)

References 9 publications

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“…The experiments performed here further show that the small intestinal N-acetyl-/5-glucosaminidase possesses characteristics similar to that in other tissues. The pH optimum is similar to that found for different tissues by Findlay and Levvy [7], Boroah, Leabeck and Walker [2], W alker, W oolen and H eyworth [26], Weissman et al [27], Vaes and J acques [25] and other authors. The value of Km (for N-acetyl-/5-glucosaminidase) and Ki (for acetate) reported herein agree in order of magnitude with findings of similar constants for N-acetyl-/3-glucosaminidase from other mammalian sources [7,20,26,27], In agreement with Levvy [14] and Conchie et al [5] saccharolactone also does not affect this enzyme in the small intestine, inhibiting the /5-glucuronidase activity as found previously [8].…”

Section: Discussionsupporting

confidence: 67%

N-Acetyl-β-Glucosaminidase in the Small Intestine and its Changes during Postnatal Development of the Rat

Koldovský¹,

Herbst²

1971

Neonatology

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Section: Discussionsupporting

confidence: 67%

N-Acetyl-β-Glucosaminidase in the Small Intestine and its Changes during Postnatal Development of the Rat

Koldovský¹,

Herbst²

1971

Neonatology

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“…[25][26][27][28] The detection of enzyme activity through an efficient and simple design is therefore of utmost importance. The most commonly employed enzyme assays are solution based and the detection is done either through colorimetry [29][30][31][32][33] or fluorimetry. 34,35 Although the fluorescence based assays provide a higher intrinsic sensitivity, the autofluorescence from biological samples interferes with the measurements and this is a drawback for the detection of bioanalytes.…”

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confidence: 99%

Supramolecular Approach to Enzyme Sensing on Paper Discs Using Lanthanide Photoluminescence

Gorai

Maitra

2016

ACS Sens.

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A paper based photoluminescent biosensor has been developed, with green Tb-luminescence as the output, for the rapid detection of β-glucosidase and lipase, both in purified form and in biological/natural fluids. A Tb Cholate hydrogel doped with specially designed, specific enzyme substrates (″pro″-sensitizers) was integrated on filter paper discs.The addition of small volumes (∼5 μL) of enzyme solutions on these discs led to enhanced green emission (UV lamp, λex 365 nm), allowing qualitative detection of the enzymeswhen needed, the intensity enhancement can be quantified using image processing software, or for multiple samples using a commercial plate reader. This simple technique allowed the detection of β-glucosidase in almond extract and lipase in blood serum. Easy identification of the inhibition of β-glucosidase was also demonstrated. The paper based sensor is inexpensive, user-friendly and needs low volumes of biological sample for analysis. This strategy has the potential to be useful for possible clinical applications.

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“…The activity of the lysosomal marker, N-acetyl-/?-glucosoaminidase, in the subcellular fractions of the liver was measured by the method of Borooah et al [7] in the presence of Triton X-100 (0.10/, final concentration) using pnitrophenyl-2 -acetamido -2 -deoxy-p-D-ghcopyranoside as substrate. The activity was expressed as p-nitrophenol liberated in pg x g liver-I x min-I at 37 "C. The activity of the mitochondria1 marker, suc-…”

Section: Enzyme Activitymentioning

confidence: 99%

Fate of Protein‐Containing Liposomes Injected into Rats

Gregoriadis

Ryman

1972

European Journal of Biochemistry

317

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[3H]Amyloglucosidase and 1311-labelled albumin were entrapped into liposomes (lipid spherules) composed of phosphatidyl choline, cholesterol and dicetyl phosphate (7 : 2 : 1 molar ratio). l3lI-labelled albumin was also entrapped in [3H]cholesterol-liposomes.Investigations on the fate in vivo following intravenous injection of such protein-containing liposomes into rats, showed that the bulk of liposomal radioactivity is removed from the blood within minutes. There is no measurable leakage of entrapped 1311-labelled albumin while liposomes are in the circulation.Most of the removed liposomal radioactivity was recovered in the liver. Autoradiographic examination of the liver 3 min after injection of albumin-containing [3H]cholesterol-liposomes suggests that hepatocytes and probably Kupffer cells are involved in the uptake of liposomes. It appears that liposomes enter this tissue intact but subsequently liposomal membranes and entrapped protein are catabolized.These catabolic processes are probably occurring in the liver lysosomes, as most of the liposoma1 radioactivity in this tissue was recovered in the mitochondrial-lysosomal fraction. Liposomes appear to be promising as a vehicle for the administration of enzymes and possibly also drugs to patients with storage diseases.In previous work [l] we reported the entrapment of albumin and Aspergillus niger amyloglucosidase into liposomes. Liposomes are lipid spherules formed when phospholipids are allowed to swell in aqueous media and become hydrated crystals [2,3].

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Studies on glucosaminidase. 2. Substrates for N-acetyl-β-glucosaminidase

Cited by 96 publications

References 9 publications

N-Acetyl-β-Glucosaminidase in the Small Intestine and its Changes during Postnatal Development of the Rat

N-Acetyl-β-Glucosaminidase in the Small Intestine and its Changes during Postnatal Development of the Rat

Supramolecular Approach to Enzyme Sensing on Paper Discs Using Lanthanide Photoluminescence

Fate of Protein‐Containing Liposomes Injected into Rats

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