Abstract:
:We cloned and sequenced a full-length cDNA of human placental N-acetylgalactosamine-6-sulfate sulfatase, the enzyme deficient in Morquio disease. The 2339-nucleotide sequence contained 1566 nucleotides which encoded a polypeptide of 522 amino acid residues. The deduced amino acid sequence was composed of a 26-amino acid N-terminal signal peptide and a mature polypeptide of 496 amino acid residues including two potential asparagine-linked glycosylation sites. Expression of the cDNA in transfected deficient fibroblasts resulted in higher production of this sulfatase activity than in untransfected deficient fibroblasts. The cDNA clone was hybridized to only a 2.3-kilobase species of RNA in human fibroblasts. The amino acid sequence of N-acetylgalactosamine-6-sulfate sulfatase showed a high degree of homology with those of other sulfatases such as human arylsulfatases A, B or C, glucosamine-6-sulfatase, iduronate-2-sulfatase and sea urchin arylsulfatase.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Tomatsu S,Fukuda S,Masue M,Sukegawa K,Fukao T,Yamagishi A,Hori T,Iwata H,Ogawa T,Nakashima Ydoi
10.1016/0006-291x(91)91244-7subject
Has Abstract,Author List Incompletepub_date
1991-12-16 00:00:00pages
677-83issue
2eissn
0006-291Xissn
1090-2104pii
0006-291X(91)91244-7journal_volume
181pub_type
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