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Cytidine monophospho-N-acetylneuraminic acid
(CMP-NeuAc) hydroxylase, which is the key enzyme for the synthesis of N-glycolylneuraminic acid (NeuGc), has been purified from the
cytosolic fraction of mouse liver, as described in our previous paper.
The amino acid sequences of the purified CMP-NeuAc hydroxylase, and
peptides obtained by lysylendopeptidase digestion, were used to
synthesize specific oligonucleotide primers. A mouse cDNA clone of the
enzyme was obtained by a combination of the polymerase chain reaction
and rapid amplification of cDNA ends. The sequence of the clone
contained an open reading frame coding for a protein of 577 amino acids
with a predicted molecular mass of 66 kDa. The deduced sequence
included the amino acid sequences obtained for the purified enzyme and
peptides, and a complete match was obtained for 159 residues. The
enzyme has neither a signal peptide sequence nor a membrane spanning
domain, which is consistent with localization of the enzyme in the
cytosol. Transfection of a cDNA construct to COS-1 cells increased the
enzyme activity and the amount of NeuGc. Comparison of the sequence
with GenBank data indicated that no similar sequence has been reported
so far. Northern blot analysis of various mouse tissues with the enzyme
cDNA as a probe indicated that expression of NeuGc is related to the
level of CMP-NeuAc hydroxylase mRNA. On Southern blot analysis with the
same probe, cross-hybridizing bands were detected in the human and fish
genomes.
Volume 270,
Number 27,
Issue of July 07, pp. 16458-16463, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
REGULATION OF SPECIES- AND TISSUE-SPECIFIC EXPRESSION OF N-GLYCOLYLNEURAMINIC ACID
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