Consequences of the Endogenous N-Glycosylation of Human Ribonuclease 1.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
19 02 2019
19 02 2019
Historique:
pubmed:
12
1
2019
medline:
27
11
2019
entrez:
12
1
2019
Statut:
ppublish
Résumé
Ribonuclease 1 (RNase 1) is the most prevalent human homologue of the archetypal enzyme RNase A. RNase 1 contains sequons for N-linked glycosylation at Asn34, Asn76, and Asn88 and is N-glycosylated at all three sites in vivo. The effect of N-glycosylation on the structure and function of RNase 1 is unknown. By using an engineered strain of the yeast Pichia pastoris, we installed a heptasaccharide (Man
Identifiants
pubmed: 30633504
doi: 10.1021/acs.biochem.8b01246
pmc: PMC6380942
mid: NIHMS1008659
doi:
Substances chimiques
RNA, Double-Stranded
0
Recombinant Proteins
0
Asparagine
7006-34-0
Ribonuclease, Pancreatic
EC 3.1.27.5
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
987-996Subventions
Organisme : NCI NIH HHS
ID : R01 CA073808
Pays : United States
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