Characterization of beta 1----4 galactosyltransferase purified from rat liver microsomes.

Abstract

beta 1----4 Galactosyltransferase was purified from rat liver microsomes. Catalytic properties of the enzyme resembled those of previously purified soluble and membrane-bound beta 1----4 galactosyltransferases. The enzyme purified in the present study showed a major band around a molecular weight of 53,000 on SDS-PAGE. The NH2-terminal sequence of the enzyme was determined up to the 20th residue. The sequence was identical to the amino acid sequence from Ala-13 to Lys-32 deduced from mouse beta 1----4 galactosyltransferase cDNA. These results suggest that most of the mature enzyme in rat liver microsomes is produced by removal of the NH2-terminal 12 amino acids from a precursor polypeptide.

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@article{Kawano1992CharacterizationOB, title={Characterization of beta 1----4 galactosyltransferase purified from rat liver microsomes.}, author={Jun-ichi Kawano and Tsutomu Oinuma and Tomohiro Nakayama and Tatsuo Suganuma}, journal={Journal of biochemistry}, year={1992}, volume={111 5}, pages={568-72} }