A Scj1p Homolog and Folding Catalysts Present in Dog Pancreas Microsomes
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Christiane Bies
Abstract
Dog pancreas microsomes represent the key components of the established model system for the analysis of protein transport into the mammalian endoplasmic reticulum. More recently, these microsomes were also employed in cell-free systems which address questions related to protein folding and protein degradation in the mammalian endoplasmic reticulum. In order to get at a complete picture of these undoubtedly related processes in the in vitro system we need to know all the proteins we are dealing with, and their respective stoichiometries. Here we give a progress report on our attempts to identify and to quantify the soluble molecular chaperones and folding catalysts which are present in the lumen of dog pancreas microsomes. Eventually, we will need to know how the in vitro system compares with the situation in intact pancreatic cells as well as in other cells.
Copyright © 1999 by Walter de Gruyter GmbH & Co. KG
Articles in the same Issue
- Editors Note
- Walter Neupert: Spellbound by Mitochondria
- Posttranslational Protein Translocation Across the Membrane of the Endoplasmic Reticulum
- Import of Carrier Proteins into Mitochondria
- The Essential Role of Mitochondria in the Biogenesis of Cellular Iron-Sulfur Proteins
- Mitochondrial Iron Metabolism in the Yeast Saccharomyces cerevisiae
- A Scj1p Homolog and Folding Catalysts Present in Dog Pancreas Microsomes
- The Import Pathway of Human and Thermoplasma 20S Proteasomes into HeLa Cell Nuclei Is Different from That of Classical NLS-Bearing Proteins
- Role of p52 (NF-kappaB2) in LPS Tolerance in a Human B Cell Line
- SHP1 Protein Tyrosine Phosphatase Negatively Modulates Erythroid Differentiation and Suppression of Apoptosis in J2E Erythroleukemic Cells
- Comparative Cleavage Sites within the Reactive-Site Loop of Native and Oxidized α1-Proteinase Inhibitor by Selected Bacterial Proteinases
- A High Affinity Binding Site for the Polypyrimidine Tract Binding Protein (PTB) Is Located in the 5'-Untranslated Region of the Rat Proteinase α1-Inhibitor 3 Variant I Gene
- Defining the Location and Function of Domains of McrB by Deletion Mutagenesis
- Disruption of the Gene for Hsp30, an α-Crystallin-Related Heat Shock Protein of Neurospora crassa, Causes Defects in Import of Proteins into Mitochondria
- Cloning, Purification and Characterisation of Cystathionine γ-Synthase from Nicotiana tabacum
- Isolation and Characterization of Viridin, a New 65 kDa Antifungal Protein from the Mould Trichoderma viride
- The T-Knot Motif Revisited
Articles in the same Issue
- Editors Note
- Walter Neupert: Spellbound by Mitochondria
- Posttranslational Protein Translocation Across the Membrane of the Endoplasmic Reticulum
- Import of Carrier Proteins into Mitochondria
- The Essential Role of Mitochondria in the Biogenesis of Cellular Iron-Sulfur Proteins
- Mitochondrial Iron Metabolism in the Yeast Saccharomyces cerevisiae
- A Scj1p Homolog and Folding Catalysts Present in Dog Pancreas Microsomes
- The Import Pathway of Human and Thermoplasma 20S Proteasomes into HeLa Cell Nuclei Is Different from That of Classical NLS-Bearing Proteins
- Role of p52 (NF-kappaB2) in LPS Tolerance in a Human B Cell Line
- SHP1 Protein Tyrosine Phosphatase Negatively Modulates Erythroid Differentiation and Suppression of Apoptosis in J2E Erythroleukemic Cells
- Comparative Cleavage Sites within the Reactive-Site Loop of Native and Oxidized α1-Proteinase Inhibitor by Selected Bacterial Proteinases
- A High Affinity Binding Site for the Polypyrimidine Tract Binding Protein (PTB) Is Located in the 5'-Untranslated Region of the Rat Proteinase α1-Inhibitor 3 Variant I Gene
- Defining the Location and Function of Domains of McrB by Deletion Mutagenesis
- Disruption of the Gene for Hsp30, an α-Crystallin-Related Heat Shock Protein of Neurospora crassa, Causes Defects in Import of Proteins into Mitochondria
- Cloning, Purification and Characterisation of Cystathionine γ-Synthase from Nicotiana tabacum
- Isolation and Characterization of Viridin, a New 65 kDa Antifungal Protein from the Mould Trichoderma viride
- The T-Knot Motif Revisited
