Article
Secretion of active kringle-2-serine protease in Escherichia coli.
Biochemistry - 16 Oct 1990
Obukowicz M G, Gustafson M E, Junger K D, Leimgruber R M, Wittwer A J, Wun T C, Warren T G, Bishop B F, Mathis K J, McPherson D T
Abstract excerpt
Active human tissue plasminogen activator variant kringle-2-serine protease (K2 + SP domains; referred to as MB1004) was synthesized as a secreted protein in Escherichia coli, isolated, and characterized. MB1004 is a relatively large and complex protein, approximately 38 kDa in size and containin...
Topics
- Base Sequence
- Blotting, Western
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Genetic Variation
- Glycosylation
- Humans
- Molecular Sequence Data
- Molecular Weight
- Oligonucleotide Probes
- Plasmids
- Recombinant Proteins
- Restriction Mapping
- Serine Endopeptidases
- Tissue Plasminogen Activator