Abstract
Galactosyltransferase specific activities in embryonic chick retina, optic tectum, and telencephalon were found to decline during embryonic development. Incorporation of galactose from nucleotide sugar into exogenously added glycoprotein acceptor was measured in the presence of excess of glycoprotein acceptor. This ensured that the specific activity measurements were reflections of tru enzyme specific activity rather than availability of acceptor. Moreover, we have shown that the decline in specific activity is not due to degradation of the nucleotide sugar, UDP-galactose, under our in vitro assay conditions. Enzymatic specific activity declined sharply with embryonic age for all tissues tested. This decline was not affected by the presence of 5-bromodeoxyuridine during in vitro culture of embryonic chick neural retina above that caused by the culturing alone. Galactosyltransferase activity was not found to be associated with the plasma membrane fraction from homogenized tissue but rather with the microsomal fraction. Thus, the changes in galactosyltransferase specific activity detected here do not reflect changes at the cell surface.
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