Purification and characterization of a beta-glucuronidase present during embryogenesis of the mollusk Pomacea sp.
A beta-glucuronidase was purified from Pomacea sp. eggs by ammonium sulfate fractionation, DEAE-BioGel and Heparin-Sepharose chromatographies. This enzyme showed a Mr 180 kDa, with subunits of 90 kDa. The kinetic parameters were: pH 4.0, temperature 60 degrees C, Km 2.7 x 10(-6) and Vmax 15.3 microM/h, activator Mg+2, and inhibitor: lactone of D-saccharic acid. beta-glucuronidase is an exoglucuronidase involved in glycosaminoglycans metabolism with kinetics parameters similar to those found in mammals.
Pereira
Wogelsanger O
WO
Departamento de Bioquímica, Centro de Biociencias, Universidade Federal do Rio Grande do Norte, 59072-970, Natal/RN, Brazil.
Cruz
Ana K M
AK
Albuquerque
Elizabeth M M
EM
Santos
Elizeu A
EA
Oliveira
Adeliana S
AS
Sales
Mauricio P
MP
Oliveira
Fernanda W
FW
D000818:Animals; D047108:Embryonic Development; D004795:Enzyme Stability; D005966:Glucuronidase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D008974:Mollusca / Q000145:classification / Q000196:embryology* / Q000201:enzymology*; D013696:Temperature
D005966:Glucuronidase