ISSN:
1471-4159
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
Abstract— The properties of rat CNS UDP-galactose-ceramidc galactosyltransferase in an axolemma-enriched fraction (AXL), microsomes, and myelin simultaneously isolated with the AXL was characterized using a newly developed assay system. The microsomal enzyme utilized either magnesium or manganese equally well as the divalent cation at 3.3 mm, while both the myelin and AXL enzyme preferred manganese over magnesium at this concentration. The microsomal enzyme was more stable to heat inactivation than the myelin or AXL enzyme. The AXL galactosyltransferase had the highest specific activity at 15 days (8-fold higher than that of the microsomes) and dramatically decreased in specific activity with development. The developmental profile of the myelin enzyme paralleled that of the AXL although the absolute specific activity was lower than that of AXL. In contrast, the specific activity of microsomal enzyme was quite low at the earliest age then sharply increased to 25 days and gradually decreased with further development. The specific activity of the enzyme in AXL isolated from Quaking mouse was dramatically decreased (about 5% of control levels) whereas both whole homogenate and microsomal specific activity were decreased to 35% of control levels. These data indicate that AXL and myelin contain a galactosyltransferase with properties which are unique relative to those of the microsomal fraction. The possible functional significance of these findings with respect to myelination is discussed.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1471-4159.1979.tb11044.x
