Properties of soluble fusions between mammalian aspartic proteinases and bacterial maltose-binding protein

Engineering & Materials Science

• Maltose 100%
• Carrier Proteins 88%
• Peptide Hydrolases 83%
• Fusion reactions 44%
• Sedimentation 15%
• Cathepsins 13%
• Proteolysis 11%
• Polypeptides 9%
• Dimers 9%
• Escherichia coli 7%
• Urea 7%
• Bacteria 6%
• Proteins 5%
• Agglomeration 5%

Medicine & Life Sciences

• Aspartic Acid Proteases 80%
• Maltose-Binding Proteins 80%
• Bacterial Proteins 67%
• procathepsin D 33%
• Pepsinogen A 26%
• 5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate) 11%
• Amylose 9%
• pepstatin 9%
• Endopeptidase K 8%
• Cathepsin D 8%
• Escherichia coli Proteins 7%
• Inclusion Bodies 7%
• Urea 5%
• Proteolysis 5%
• Bacteria 4%
• Peptides 3%
• Proteins 2%

Chemical Compounds

• Protein 22%
• Sedimentation 11%
• Pepstatin 9%
• Amylose 7%
• Hydrophobic Surface 6%
• Protein Hydrolysis 6%
• Polypeptide 5%
• Enzyme Activity 5%
• Urea 4%