Characterization of beta 1----4 galactosyltransferase purified from rat liver microsomes.
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.
Kawano
J
J
Department of Anatomy, Miyazaki Medical College.
Oinuma
T
T
Nakayama
T
T
Suganuma
T
T
D000595:Amino Acid Sequence; D000818:Animals; D004792:Enzyme Precursors / Q000235:genetics; D005700:Galactosyltransferases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D008862:Microsomes, Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains; D012689:Sequence Homology, Nucleic Acid
D004792:Enzyme Precursors; D005700:Galactosyltransferases