Separation and properties of β-galactosidase, β-glucosidase, β-glucuronidase and N-acetyl-β-glucosaminidase from rat kidney

Abstract

1. The activities of beta-galactosidase, beta-glucosidase, beta-glucuronidase and N-acetyl-beta-glucosaminidase from rat kidney have been compared when 4-methylumbelliferyl glycosides are used as substrates. 2. Separation by gel electrophoresis at pH7.0 indicated slow- and fast-moving components of rat-kidney beta-galactosidase. 3. The fast-moving component is also associated with the total beta-glucosidase activity and inhibition experiments indicate that a single enzyme species is responsible for both activities. 4. DEAE-cellulose chromatography and filtration on Sephadex gels suggests that the beta-glucosidase component is a small acidic molecule, of molecular weight approx. 40000-50000, with optimum pH5.5-6.0 for beta-galactosidase and beta-glucosidase activities. 5. The major beta-galactosidase component has low electrophoretic mobility, a calculated molecular weight of 80000 and optimum pH3.7.

Gargoylism: hydrolysis of β-galactosides and tissue accumulation of galactose- and mannose-containing compounds

“…Several reports have been published in which P-galactosidase activity in various human and animal tissues has been studied. Different substrates have been used such as lactose, synthetic heterogalactosides (MU-i3-galactoside, ONP-P-galactoside, PNP-fgalactoside) (2,(21)(22)(23), and naturally occurring P-galactosides, ceramide P-lactoside (17,(24)(25)(26)(27) and sialic acidfree ai-acid glycoprotein (28,29). Keratan sulfate does not seem to have been studied earlier in this respect.…”

Recruitment of predators and parasitoids by herbivore-injured plants

“…Beta-glucosidases are present in many organisms (e.g., Robinson et al, 1967;Sano et al, 1975;Wertz and Downing, 1989;Yu, 1989) and may function in catalyzing biochemical pathways that involve glycoside cleavage. The emissions by Brassicaceae are characterized by glucosinolate breakdown products, which have not been observed in other plant families that have been studied in this context (Agelopoulos and Keller, 1994;Mattiaci et al, 1994;Geervliet et al, 1996).…”

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

“…N-acetyl-/?-glucosaminidase has been detected in many tissues of the rat [5] and extensively studied mainly in the liver [24,27], kidney [23,26], bone [25], spleen [22], testis [4,29] and epididymis [7]. Although Conchie et al [5] in the survey of rat tissues noted the presence of the enzyme in the intestine, there has been no detailed studies on the N-acetyl-/i-glucosaminidase in this tissue.…”