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

Structural characterization of recombinant consensus interferon-alpha.

M L Klein1, T D Bartley, P H Lai

  • 1Amgen Inc., Thousand Oaks, CA 91320.

Journal of Chromatography
|November 11, 1988
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

The antibody-peptide fusion protein, AT-02, is an effective opsonin with pan-amyloid reactivity.

npj drug discovery·2026
Same author

[Auxiliary pathological diagnosis algorithm based on color moments for frozen-section of thyroid cancer].

Zhonghua bing li xue za zhi = Chinese journal of pathology·2021
Same author

Modification of the double purse-string suture for the excision of a large pigmented naevus on the buttock.

Clinical and experimental dermatology·2016
Same author

[Clinical characteristics and outcomes of patients with acute aortic dissection: impact of hypertension].

Zhonghua xin xue guan bing za zhi·2016
Same author

Evaluation of an Intracranial Arteriovenous Malformation by Multi-Detector CT Angiography. A Case Report.

The neuroradiology journal·2013
Same author

An undescribed coexistence of benign metastasizing leiomyoma in the lung with serous borderline tumor of the ovary.

European journal of gynaecological oncology·2013

Recombinant consensus interferon-alpha, produced using genetically modified E. coli, was structurally characterized. Its amino acid sequence and disulfide linkages were confirmed, validating the synthetic gene

Area of Science:

  • Biotechnology
  • Molecular Biology
  • Protein Chemistry

Background:

  • Interferon-alpha plays a crucial role in the immune response.
  • Developing recombinant versions allows for therapeutic applications.

Purpose of the Study:

  • To structurally characterize recombinant consensus interferon-alpha.
  • To confirm the integrity and biological activity of the synthesized protein.

Main Methods:

  • Genetic modification of Escherichia coli for protein expression.
  • Purification and biological activity assessment.
  • Detailed structural characterization including sequence determination and peptide analysis.

Main Results:

  • The purified protein was biologically active and homogeneous.

Related Experiment Videos

  • Two homologous polypeptides were identified, differing by a single N-terminal methionyl residue.
  • The amino acid sequence matched the synthetic gene's coding sequence.
  • Two intramolecular disulfide linkages (Cys(1)-Cys(99) and Cys(29)-Cys(139)) were confirmed.

    • Conclusions:

    • The structural characterization confirms the successful production of recombinant consensus interferon-alpha.
    • The protein's sequence and disulfide bonds are consistent with its expected structure and function.