Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Human cathepsin E produced in E. coli

J Hill1, D S Montgomery, J Kay

  • 1Department of Biochemistry, University of Wales College, Cardiff, UK.

FEBS Letters
|July 12, 1993
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Achievement of Target Gain Larger than Unity in an Inertial Fusion Experiment.

Physical review letters·2024
Same author

Monte Carlo N-Particle forward modeling for density reconstruction of double shell capsule radiographs.

The Review of scientific instruments·2022
Same author

Lawson Criterion for Ignition Exceeded in an Inertial Fusion Experiment.

Physical review letters·2022
Same author

Erratum: Measurement of Preheat Due to Nonlocal Electron Transport in Warm Dense Matter [Phys. Rev. Lett. 120, 025002 (2018)].

Physical review letters·2020
Same author

Direct-drive double-shell implosion: A platform for burning-plasma physics studies.

Physical review. E·2020
Same author

Measurement of Preheat Due to Nonlocal Electron Transport in Warm Dense Matter.

Physical review letters·2018
Same journal

Identification of a Shiga toxin A-derived peptide internalized into Gb3 receptor-bearing cells via interaction with the Shiga toxin B subunit.

FEBS letters·2026
Same journal

The dual role of lectins in cancer-immunotherapy tools and therapeutic targets.

FEBS letters·2026
Same journal

Decoding the dynamic extracellular matrix in cancer-3D models and bioscaffolds rewire the rules of tumor progression.

FEBS letters·2026
Same journal

Extending the classical sequence-structure-function paradigm through protein dynamics and context-dependent behavior.

FEBS letters·2026
Same journal

α-Synuclein aggregation landscape from phase separation to neurotoxic intermediates.

FEBS letters·2026
Same journal

Modelling stem cell differentiation related processes-A practical overview for biologists.

FEBS letters·2026
See all related articles

Researchers successfully produced recombinant procathepsin E from human gastric cells in E. coli. This purified enzyme shows similar properties to the natural form, enabling further structural and activity studies.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Procathepsin E is an aspartic protease implicated in various physiological and pathological processes.
  • Efficient production of active recombinant enzymes is crucial for detailed biochemical and structural studies.

Purpose of the Study:

  • To develop a method for producing active recombinant human procathepsin E in Escherichia coli (E. coli).
  • To characterize the properties of the recombinant enzyme and assess its suitability for further structural and functional analysis.

Main Methods:

  • Complementary DNA (cDNA) for procathepsin E was synthesized from human gastric adenocarcinoma (AGS) cells.
  • The cDNA was amplified using the polymerase chain reaction (PCR) and cloned into the pET 22b vector for expression in E. coli.

Related Experiment Videos

  • Recombinant protein purification was achieved without column chromatography.

    • Main Results:

    • Homogeneous active recombinant procathepsin E was obtained with a yield of approximately 3 mg per 40 g of cells.
    • The purified recombinant enzyme exhibited properties comparable to the naturally occurring human procathepsin E.
    • The yield and purity are sufficient for initiating crystallization, structural analysis, and mutagenesis studies.

    Conclusions:

    • A straightforward and efficient method for producing active recombinant human procathepsin E has been established.
    • The recombinant enzyme serves as a valuable tool for future investigations into its structure-activity relationships.
    • This work facilitates detailed structural and functional characterization of procathepsin E.