{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,9]],"date-time":"2025-11-09T07:40:51Z","timestamp":1762674051826},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1995,10,1]]},"abstract":"<jats:p>Full-length cDNA sequences encoding human N-acetylgalactosamine-6-sulphatase were stably expressed in Chinese hamster ovary cells under the transcriptional control of the human polypeptide chain elongation factor 1 alpha gene promoter. A clonal cell line overexpressing recombinant N-acetylgalactosamine-6-sulphatase to a level of approx. 3 mg\/l of culture medium was isolated. The secreted precursor enzyme was purified to homogeneity by a two-column procedure with an overall yield of 53% of the activity. The physical and catalytic parameters of the recombinant enzyme were similar to those of the mature form isolated from liver. On SDS\/PAGE and gel filtration, recombinant N-acetylgalactosamine-6-sulphatase had a native molecular mass of 58-60 kDa. Recombinant N-acetylgalactosamine-6-sulphatase was endocytosed by mucopolysaccharidosis IVA fibroblasts via the mannose-6-phosphate receptor-mediated pathway and was efficiently localized to lysosomes.<\/jats:p>","DOI":"10.1042\/bj3110333","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:45:43Z","timestamp":1439243143000},"page":"333-339","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":31,"title":["Expression, purification and characterization of recombinant human <i>N<\/i>-acetylgalactosamine-6-sulphatase"],"prefix":"10.1042","volume":"311","author":[{"given":"J","family":"Bielicki","sequence":"first","affiliation":[{"name":"Lysosomal Diseases Research Unit, Department of Chemical Pathology, Women's and Children's Hospital, 72 King William Road, North Adelaide, South Australia 5006, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M","family":"Fuller","sequence":"additional","affiliation":[{"name":"Lysosomal Diseases Research Unit, Department of Chemical Pathology, Women's and Children's Hospital, 72 King William Road, North Adelaide, South Australia 5006, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"X H","family":"Guo","sequence":"additional","affiliation":[{"name":"Lysosomal Diseases Research Unit, Department of Chemical Pathology, Women's and Children's Hospital, 72 King William Road, North Adelaide, South Australia 5006, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C P","family":"Morris","sequence":"additional","affiliation":[{"name":"Lysosomal Diseases Research Unit, Department of Chemical Pathology, Women's and Children's Hospital, 72 King William Road, North Adelaide, South Australia 5006, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J J","family":"Hopewood","sequence":"additional","affiliation":[{"name":"Lysosomal Diseases Research Unit, Department of Chemical Pathology, Women's and Children's Hospital, 72 King William Road, North Adelaide, South Australia 5006, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D S","family":"Anson","sequence":"additional","affiliation":[{"name":"Lysosomal Diseases Research Unit, Department of Chemical Pathology, Women's and Children's Hospital, 72 King William Road, North Adelaide, South Australia 5006, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/311\/1\/333\/618239\/bj3110333.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/311\/1\/333\/618239\/bj3110333.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T23:44:36Z","timestamp":1637711076000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/311\/1\/333\/32038\/Expression-purification-and-characterization-of"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,10,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1995,10,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3110333","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1995,10,1]]}}}