{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,10,28]],"date-time":"2023-10-28T05:40:37Z","timestamp":1698471637388},"reference-count":0,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2008,1,16]],"date-time":"2008-01-16T00:00:00Z","timestamp":1200441600000},"content-version":"vor","delay-in-days":4216,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IUBMB Life"],"published-print":{"date-parts":[[1996,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Glycogen debranching enzyme and acid \u03b1\u2010glucosdase are responsible for glycogen degradation in human. The formal enzyme is a mulifunctional enzyme with two independenent catalytic activities occuring on a single polypeptide, while the latter is a lysosomal enzyme which matures through extensive glycosylation and phosphorylation and proteolytic processing. Deficiency of glycogen debranching enzyme and acid \u03b1\u2010glucosidase cause glycogen storage disease type III and II, respectively. Baculovirus\/insect expression system was used to produce both GDE and GAA. Both enzymes were found to be catalytically and antigenically active. The majority of recombinant GDE is present in the medium (70%). Uptake experiment indicated that GAA produced in the insect cells could not be absorbed into the GSD type II patient fiboblasts through mannose\u20106\u2010phosphate receptor mediated endocytosis. Uptake experiment combined with immunoblot analysis indicated there are differences in the posttranslational modification and processing between insect cells and mammalian cells.<\/jats:p>","DOI":"10.1080\/15216549600201841","type":"journal-article","created":{"date-parts":[[2007,7,7]],"date-time":"2007-07-07T11:37:25Z","timestamp":1183808245000},"page":"755-764","source":"Crossref","is-referenced-by-count":0,"title":["Expression of catalytically active human multifunctional glycogen\u2010debranching enzyme and lysosomal acid alpha\u2010glucosidase in insect cells"],"prefix":"10.1002","volume":"39","author":[{"given":"Jer\u2010Yuarn","family":"Wu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Johan L. K.","family":"Van Hove","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yuan\u2010Sheng","family":"Huang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yuan\u2010Tsong","family":"Chen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,1,16]]},"container-title":["IUBMB Life"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1080%2F15216549600201841","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/iubmb.onlinelibrary.wiley.com\/doi\/pdf\/10.1080\/15216549600201841","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,27]],"date-time":"2023-10-27T03:38:56Z","timestamp":1698377936000},"score":1,"resource":{"primary":{"URL":"https:\/\/iubmb.onlinelibrary.wiley.com\/doi\/10.1080\/15216549600201841"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996,7]]},"references-count":0,"journal-issue":{"issue":"4","published-print":{"date-parts":[[1996,7]]}},"alternative-id":["10.1080\/15216549600201841"],"URL":"https:\/\/doi.org\/10.1080\/15216549600201841","archive":["Portico"],"relation":{},"ISSN":["1521-6543","1521-6551"],"issn-type":[{"value":"1521-6543","type":"print"},{"value":"1521-6551","type":"electronic"}],"subject":[],"published":{"date-parts":[[1996,7]]}}}