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Human cathepsin G lacking functional glycosylation site is proteolytically processed and targeted for storage in granules after transfection to the rat basophilic/mast cell line RBL or the murine myeloid cell line 32D
Lunds universitet.
1995 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 270, no 47, 28413-28418 p.Article in journal (Refereed) Published
Place, publisher, year, edition, pages
1995. Vol. 270, no 47, 28413-28418 p.
Keyword [en]
Amino Acid Sequence, Animals, Base Sequence, Cathepsins/*biosynthesis/isolation & purification, Cell Line, Chromatography; Affinity, Cytoplasmic Granules/*metabolism, DNA Primers, Glutamine, Glycosylation, Humans, Kinetics, Leukemia; Basophilic; Acute, Mast Cells, Mice, Molecular Sequence Data, Mutagenesis; Site-Directed, Point Mutation, Polymerase Chain Reaction, Protein Processing; Post-Translational, Rats, Recombinant Proteins/biosynthesis/isolation & purification, Sequence Deletion, Serine Endopeptidases, Transfection, Tumor Cells; Cultured
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Medical and Health Sciences Natural Sciences
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URN: urn:nbn:se:uu:diva-17327DOI: 10.1074/jbc.270.47.28413ISI: A1995TG21000071PubMedID: 7499346OAI: oai:DiVA.org:uu-17327DiVA: diva2:45098
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Publikation från annat universitet

Available from: 2008-06-18 Created: 2008-06-18 Last updated: 2017-12-08

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Garwicz, Daniel

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