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The hydrophobic repeated domain of the Clostridium cellulovorans cellulose-binding protein (CbpA) has specific interactions with endoglucanases
- Source :
- Journal of Bacteriology. 175:7119-7122
- Publication Year :
- 1993
- Publisher :
- American Society for Microbiology, 1993.
-
Abstract
- We overexpressed one of the hydrophobic repeated domains (HBDs) (110 amino acid residues) of the cellulose-binding protein (CbpA) from Clostridium cellulovorans by making a hybrid protein with the Escherichia coli maltose-binding protein (MalE). The HBD was purified to homogeneity, and interactions between the HBD and endoglucanases were analyzed by a novel interaction Western blotting (immunoblotting) method. The HBD had specific interactions with endoglucanases (EngB and EngD) from C. cellulovorans. These results indicated that the HBD was an endoglucanase binding site of CbpA.
- Subjects :
- Monosaccharide Transport Proteins
Recombinant Fusion Proteins
Two-hybrid screening
Blotting, Western
Molecular Sequence Data
Restriction Mapping
Cellulase
medicine.disease_cause
Microbiology
Maltose-Binding Proteins
Immunoenzyme Techniques
Bacterial Proteins
medicine
Binding site
Molecular Biology
Escherichia coli
Clostridium cellulovorans
Repetitive Sequences, Nucleic Acid
Clostridium
chemistry.chemical_classification
Binding Sites
Base Sequence
biology
Escherichia coli Proteins
Binding protein
Cellulose binding
biology.organism_classification
Enzyme
Biochemistry
chemistry
Periplasmic Binding Proteins
Protein Biosynthesis
biology.protein
ATP-Binding Cassette Transporters
Electrophoresis, Polyacrylamide Gel
Carrier Proteins
Research Article
Subjects
Details
- ISSN :
- 10985530 and 00219193
- Volume :
- 175
- Database :
- OpenAIRE
- Journal :
- Journal of Bacteriology
- Accession number :
- edsair.doi.dedup.....0377eeb1e09d52d9b0221d7bb1043511