Sialidase activity in nuclear membranes of rat brain.
A highly purified nuclear membrane preparation was obtained from adult rat brain and examined for sialidase activity using GM3, GD1a, GD1b, or N-acetylneuramin lactitol as the substrate. The nuclear membranes contained an appreciable level of sialidase activity; the specific activities toward GM3 and N-acetylneuramin lactitol were 20.5 and 23.8% of the activities in the total brain homogenate, respectively. The sialidase activity in nuclear membranes showed substrate specificity distinct from other membrane-bound sialidases localized in lysosomal membranes, synaptosomal plasma membranes, or myelin membranes. These results strongly suggest the existence of a sialidase activity associated with the nuclear membranes from rat brain.
Saito
M
M
Department of Biochemistry and Molecular Biophysics, Medical College of Virginia, Virginia Commonwealth University, Richmond 23298-0614, USA.
Fronda
C L
CL
Yu
R K
RK
D000818:Animals; D001921:Brain / Q000201:enzymology*; D005679:G(M3) Ganglioside / Q000378:metabolism; D009439:Neuraminidase / Q000378:metabolism*; D009685:Nuclear Envelope / Q000201:enzymology*; D051381:Rats; D017207:Rats, Sprague-Dawley; D012794:Sialic Acids / Q000378:metabolism; D013379:Substrate Specificity
D005679:G(M3) Ganglioside; D012794:Sialic Acids; C029412:neuramin lactitol; D009439:Neuraminidase