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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

Garwicz, Daniel (author)
Lunds universitet
Lindmark, A (author)
Gullberg, U (author)
 (creator_code:org_t)
Elsevier BV, 1995
1995
English.
In: Journal of Biological Chemistry. - : Elsevier BV. - 0021-9258 .- 1083-351X. ; 270:47, s. 28413-28418
  • Journal article (peer-reviewed)
Subject headings
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Keyword

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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Garwicz, Daniel
Lindmark, A
Gullberg, U
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Journal of Biolo ...
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Uppsala University

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