β-Galactosidase, β-glucosidase and N-acetyl-β-glucosaminidase in human kidney

Dance, N.; Price, Robert G.; Robinson, Donald S.; Stirling, J. L.

doi:10.1016/0009-8981(69)90311-8

Cited by 139 publications

(51 citation statements)

References 16 publications

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“…Under optimal conditions of pH anid saturatinig substrate, the enzynie assay is linear. We suspect the presence of two distinct (27) have described reaction conditions for 4MU substrates of 8-galactosidase and hexosaminidase that differ somewhat from those. In particular, the optimal (i.e., saturatinig) substrate concentration for hexosaminidase is higher than that stuggested by Dance et al (27).…”

Section: Methodsmentioning

confidence: 94%

“…We suspect the presence of two distinct (27) have described reaction conditions for 4MU substrates of 8-galactosidase and hexosaminidase that differ somewhat from those. In particular, the optimal (i.e., saturatinig) substrate concentration for hexosaminidase is higher than that stuggested by Dance et al (27). Also, the l3-galactosidase substrate concentration is lower than saturatinig dtue to linmited solubilitv of the substrate.…”

Section: Methodsmentioning

confidence: 94%

See 1 more Smart Citation

Coordinacy of lysosomal enzyme excretion in human urine.

Paigen¹,

Peterson²

1978

J. Clin. Invest.

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A B S T R A C T Assay conditions have been developed for the determination of urinary 8-glucuronidase, ,8-galactosidase, a-galactosidase, and, -hexosaminidase using fluorometric substrates. The assay conditions for ,8-glucuronidase overcome interference by both low and high molecular weight inhibitors, a problem that has confused earlier studies of enzyme excretion.The fouir lysosomal enzymes are excreted coordinately; although their absolute levels (in units per milligram of creatinine) vary during the day and from one day to the next, the ratio of one enzyme to another remains relatively constant. The lack of correlationi between plasma aind urine enzyme levels, together with the high molecular weights of these enzymes, suggests that the urinary enzymes are not derived by glomerular filtration. The lack of coordinacy with lactate dehydrogenase suggests they are not derived from exfoliated cells. By analogy with experimental animals, they' may be derived from lysosomes extruded into the lumnen of the proxinmal tubule by epithelial cells.There is considerable variation among a poptulation of 125 healthy adult subjects for total enzyme exeretionl. Both total enzyme excretion and coordinacy ratios are log-normially' distributed, suggesting that they are the resuiltants of many factors, each of which has a relative, or proportional, effect on enzyme excretion. About one-half the population variation resides in a process common to the exeretion of all four enzymes (possibly the lsosomiie extruisioni pathway'), and about one-half r-esides in factors affectiing each enzviye independently.

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Section: Methodsmentioning

confidence: 94%

Section: Methodsmentioning

confidence: 94%

Coordinacy of lysosomal enzyme excretion in human urine.

Paigen¹,

Peterson²

1978

J. Clin. Invest.

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“…It has already been reported by several investigators that there are increases in urinary activities of these enzymes when nephrotoxic agents are administered to rats (13,14) Our previous study has demonstrated that the treatment of rats with GM or HgCl2 induced sig nificantly increased urinary enzyme activities, leading to the conclusion that these activities are suitable markers for detecting nephro toxicity by nephrotoxic agents (15). In the present study, TOB, one of the AGs, was used as a nephrotoxic agent, and the pro tective effect of LMOX against TOB-induced nephrotoxicity was investigated in rats by renal histological studies and measurement of biochemical parameters including urinary LDH, NAG and LZM activities.…”

Section: Effects Of Tob Alone and In Combination Withmentioning

confidence: 86%

Studies on the Nephrotoxicity of Aminoglycoside Antibiotics and Protection from These Effects (3) Protective Effect of Latamoxef against Tobramycin Nephrotoxicity and Its Protective Mechanism

Kojima

Ito

Suzuki

1986

Japanese Journal of Pharmacology

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Abstract-Effect of latamoxef (LMOX) against tobramycin (TOB)-induced nephro toxicity was studied in rats. Treatment with TOB (90 mg/kg/day, s.c.) alone resulted in marked increases in the activities of urinary enzymes such as lactate dehydrogenase, N-acetyl-a-D-glucosaminidase and lysozyme, urinary protein content and blood urea nitrogen, which peaked on the 7th or 10th day. The combi nation with LMOX (500, 1000 or 2000 mg/kg/day, s.c.) significantly suppressed increases in the parameters with TOB alone. The extent of this suppression roughly depended on the LMOX dosage.Although TOB alone caused pronounced histo logical changes such as extensive cortical proximal tubular cell necrosis, residual tubular basement membrane and cast formations in the renal cortex and medulla on the 7th day, these changes were apparently suppressed by combination with LMOX. In addition, intrarenal TOB concentrations in the rat given TOB alone were about 350, 500 and 1000 ,rtg/g tissue wet weight at 3 hr, on day 3 and on day 5, respectively.On the other hand, there was a significant reduction (30-60%) in intrarenal TOB concentration by combination with LMOX. These results indicate that combination with LMOX obviously protects the rat kidney from TOB nephro toxicity, and the protective effect may be partially due to suppression of intrarenal accumulation of TOB by LMOX.

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“…N-acetyl-/3-hexosaminidase was assayed by the method described by Dance et al [6]. Chitobiase was assayed by incubating 100 ~1 of enzyme solution at 37°C with 100 pl 10 mM chitobiose in Mcllvaine sodium phosphate citrate buffer pH 3.5.…”

Section: Enzyme Assaysmentioning

confidence: 99%

Human N‐acetyl‐β‐hexosaminidases: Hydrolysis of N,N′diacetylchitobiose by a low molecular weight enzyme

Stirling¹

1974

FEBS Letters

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β-Galactosidase, β-glucosidase and N-acetyl-β-glucosaminidase in human kidney

Cited by 139 publications

References 16 publications

Coordinacy of lysosomal enzyme excretion in human urine.

Coordinacy of lysosomal enzyme excretion in human urine.

Studies on the Nephrotoxicity of Aminoglycoside Antibiotics and Protection from These Effects (3) Protective Effect of Latamoxef against Tobramycin Nephrotoxicity and Its Protective Mechanism

Human N‐acetyl‐β‐hexosaminidases: Hydrolysis of N,N′diacetylchitobiose by a low molecular weight enzyme

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