PubMed:15147861 JSONTXT

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":519,"end":528},"obj":"https://acgg.asia/db/ggdb/info/gg088"}],"text":"Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15.\nWe have cloned, expressed and characterized a novel member of the human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family, pp-GalNAc-T15. The pp-GalNAc-T15 transcript was ubiquitously expressed in human tissues. Recombinant pp-GalNAc-T15 transferred N-acetylgalactosamine (GalNAc) toward a panel of mucin-derived peptide substrates in vitro. Although pp-GalNAc-T15 showed significantly less catalytic activity than pp-GalNAc-T2, T15 transferred up to seven GalNAcs to the Muc5AC peptide, while T2 transferred up to five GalNAcs. These results clearly indicated that pp-GalNAc-T15 is a novel member of the human pp-GalNAc-T family with unique catalytic activity."}

{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":519,"end":528},"obj":"https://acgg.asia/db/ggdb/info/gg088"}],"text":"Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15.\nWe have cloned, expressed and characterized a novel member of the human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family, pp-GalNAc-T15. The pp-GalNAc-T15 transcript was ubiquitously expressed in human tissues. Recombinant pp-GalNAc-T15 transferred N-acetylgalactosamine (GalNAc) toward a panel of mucin-derived peptide substrates in vitro. Although pp-GalNAc-T15 showed significantly less catalytic activity than pp-GalNAc-T2, T15 transferred up to seven GalNAcs to the Muc5AC peptide, while T2 transferred up to five GalNAcs. These results clearly indicated that pp-GalNAc-T15 is a novel member of the human pp-GalNAc-T family with unique catalytic activity."}

{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":145,"end":201},"obj":"https://acgg.asia/db/ggdb/info/gg095"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":145,"end":201},"obj":"https://acgg.asia/db/ggdb/info/gg094"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":145,"end":201},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":145,"end":201},"obj":"https://acgg.asia/db/ggdb/info/gg092"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":145,"end":201},"obj":"https://acgg.asia/db/ggdb/info/gg091"},{"id":"PD-GlycoGenes20190927-B_T6","span":{"begin":145,"end":201},"obj":"https://acgg.asia/db/ggdb/info/gg090"},{"id":"PD-GlycoGenes20190927-B_T7","span":{"begin":145,"end":201},"obj":"https://acgg.asia/db/ggdb/info/gg089"},{"id":"PD-GlycoGenes20190927-B_T8","span":{"begin":145,"end":201},"obj":"https://acgg.asia/db/ggdb/info/gg088"},{"id":"PD-GlycoGenes20190927-B_T9","span":{"begin":145,"end":201},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"PD-GlycoGenes20190927-B_T10","span":{"begin":206,"end":214},"obj":"https://acgg.asia/db/ggdb/info/gg104"},{"id":"PD-GlycoGenes20190927-B_T11","span":{"begin":519,"end":528},"obj":"https://acgg.asia/db/ggdb/info/gg088"},{"id":"PD-GlycoGenes20190927-B_T12","span":{"begin":715,"end":723},"obj":"https://acgg.asia/db/ggdb/info/gg104"}],"text":"Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15.\nWe have cloned, expressed and characterized a novel member of the human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family, pp-GalNAc-T15. The pp-GalNAc-T15 transcript was ubiquitously expressed in human tissues. Recombinant pp-GalNAc-T15 transferred N-acetylgalactosamine (GalNAc) toward a panel of mucin-derived peptide substrates in vitro. Although pp-GalNAc-T15 showed significantly less catalytic activity than pp-GalNAc-T2, T15 transferred up to seven GalNAcs to the Muc5AC peptide, while T2 transferred up to five GalNAcs. These results clearly indicated that pp-GalNAc-T15 is a novel member of the human pp-GalNAc-T family with unique catalytic activity."}