Literature summary for 4.6.1.18 extracted from

Peracaula, R.; Royle, L.; Tabares, G.; Mallorqui-Fernandez, G.; Barrabes, S.; Harvey, D.J.; Dwek, R.A.; Rudd, P.M.; de Llorens, R.
Glycosylation of human pancreatic ribonuclease: differences between normal and tumor states (2003), Glycobiology, 13, 227-244.

Search for more literature for 4.6.1.18

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
14000	24000	fractions with one glycosylation site occupied, Asn34, SDS-PAGE	Homo sapiens
24000	36000	fractions with two or three glycosylation sites occupied, SDS-PAGE	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	pancreatic enzyme has three glycosylation sites, Asn34, Asn76 and Asn88. The majority of the glycans from the normal pancreas enzyme are fucosylated complex biantennary structures. Triantennary and tetrantennary fucosylated glycans are present in the highly glycosylated enzyme fractions, together with traces of glycans with poly-N-acetyllactosamine chains and others. The main core structures of the Capan-1 enzyme are hybrid glycans with branched 3-antenna and biantennary structures containing mainly Gal-GlcNAc chains, both types of compounds substituted with up to three fucose residues and some additionally sialylated. MDAPanc-3 enzyme has sialic acids and fucose linked alpha1-3 and 1-4 to the antennae and core fucose, and galactose residues linked beta1-4 to GlcNAc	Homo sapiens

Purification (Commentary)

Purification (Comment)	Organism
affinity chromatography on heparin column and reversed-phase chromatography	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
pancreas	-	Homo sapiens	-
pancreatic adenocarcinoma cell line	Capan-1 and MDAPanc-3	Homo sapiens	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)