| First Author | Tatnell PJ | Year | 1997 |
| Journal | FEBS Lett | Volume | 408 |
| Issue | 1 | Pages | 62-6 |
| PubMed ID | 9180269 | Mgi Jnum | J:40368 |
| Mgi Id | MGI:87708 | Doi | 10.1016/s0014-5793(97)00388-8 |
| Citation | Tatnell PJ, et al. (1997) Cloning, expression and characterisation of murine procathepsin E. FEBS Lett 408(1):62-6 |
| abstractText | The cDNA encoding murine procathepsin E was isolated and sequenced and recombinant enzyme was produced in Escherichia coli. The activity of the purified recombinant mouse cathepsin E was characterised quantitatively using two synthetic peptide substrates and naturally occurring inhibitors. The majority of the recombinant enzyme was present as a homodimer (Mr approximately 80) in which the two monomers were linked by an intermolecular disulfide bond. By analogy to previous studies with human cathepsin E, this is most likely a consequence of the presence of a unique cysteine residue near the N-terminus of the mature proteinase. The availability of (i) recombinant murine enzyme in reasonable quantities and (ii) a full-length cDNA now enables structural investigations and attempts to generate 'knock-out' mice deficient in this important aspartic proteinase to be undertaken. |
