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Volumn 105, Issue 1, 1987, Pages 215-227
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Two integral membrane proteins located in the cis-middle and trans-part of the Golgi system acquire sialylated N-linked carbohydrates and display different turnovers and sensitivity to cAMP-dependent phosphorylation.
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Author keywords
[No Author keywords available]
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Indexed keywords
GLYCOPROTEIN;
GOLGI MEMBRANE GLYCOPROTEINS;
MEMBRANE PROTEIN;
MONOCLONAL ANTIBODY;
N ACETYLNEURAMINIC ACID;
PHOSPHOSERINE;
PROTEIN KINASE;
PROTEIN PRECURSOR;
SIALIC ACID DERIVATIVE;
ANIMAL;
ARTICLE;
BASOPHIL;
CARBOHYDRATE METABOLISM;
CELL LINE;
EXPERIMENTAL LEUKEMIA;
FLUORESCENT ANTIBODY TECHNIQUE;
GOLGI COMPLEX;
IMMUNOLOGY;
KIDNEY;
METABOLISM;
PATHOLOGY;
PHOSPHORYLATION;
PROTEIN PROCESSING;
RAT;
ANIMALS;
ANTIBODIES, MONOCLONAL;
BASOPHILS;
CARBOHYDRATE METABOLISM;
CELL LINE;
FLUORESCENT ANTIBODY TECHNIQUE;
GLYCOPROTEINS;
GOLGI APPARATUS;
KIDNEY;
LEUKEMIA, EXPERIMENTAL;
MEMBRANE GLYCOPROTEINS;
MEMBRANE PROTEINS;
N-ACETYLNEURAMINIC ACID;
PHOSPHORYLATION;
PHOSPHOSERINE;
PROTEIN KINASES;
PROTEIN PRECURSORS;
PROTEIN PROCESSING, POST-TRANSLATIONAL;
RATS;
SIALIC ACIDS;
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EID: 0023375833
PISSN: 00219525
EISSN: None
Source Type: Journal
DOI: 10.1083/jcb.105.1.215 Document Type: Article |
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Times cited : (55)
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References (0)
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