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

The esterase-like activity of covalently bound human third complement protein.

Y P Venkatesh1, R P Levine

  • 1Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110.

Molecular Immunology
|September 1, 1988
PubMed
Summary

The complement protein C3 undergoes spontaneous hydrolysis of its acyl ester bond, catalyzed by a non-sulfhydryl group. This esterase-like activity, crucial for C3 function, is inhibited by divalent mercury and palladium ions.

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

Banana lectin (BanLec) induces non-specific activation of basophils and mast cells in atopic subjects.

European annals of allergy and clinical immunology·2018
Same author

Skin prick test analysis reveals cross-sensitization to tomato profilin and grass pollen in nasobronchialallergic patients with history of tomato food allergy.

European annals of allergy and clinical immunology·2018
Same author

Structural and functional characterization of a novel immunomodulatory glycoprotein isolated from ajowan (Trachyspermum ammi L.).

Glycoconjugate journal·2017
Same author

An overview of fruit allergy and the causative allergens.

European annals of allergy and clinical immunology·2015
Same author

Structural analyses and immunomodulatory properties of fructo-oligosaccharides from onion (Allium cepa).

Carbohydrate polymers·2014
Same author

Transcription and translation for carotenoid synthesis in Chlamydomonas reinhardtii.

Planta·2014

Area of Science:

  • Biochemistry
  • Immunology
  • Protein Chemistry

Background:

  • The third complement protein, C3, contains an acyl ester bond susceptible to spontaneous hydrolysis at neutral pH.
  • Previous studies suggested a catalytic functional group, distinct from the sulfhydryl (-SH) group, mediates this intramolecular hydrolysis.

Purpose of the Study:

  • To investigate the catalytic mechanism and identify the functional group responsible for the esterase-like activity of C3.
  • To determine the role of the sulfhydryl group and other functional groups in the hydrolytic reaction of C3.

Main Methods:

  • Inhibition studies using mercuric chloride, palladium chloride, and BAMT.
  • Covalent chromatography of C3-[3H]glycerol on organomercurial agarose.
  • Kinetic deuterium solvent isotope effect analysis.

Related Experiment Videos

Main Results:

  • Divalent mercury, palladium, and BAMT inhibited the esterase-like activity by forming complexes with the -SH group and a catalytic group (X).
  • The structural integrity of C3 essential for esterase-like activity was maintained after covalent chromatography.
  • A general-base mechanism involving catalytic group X, located in the C3d region, was proposed for the hydrolysis of the acyl ester bond.

Conclusions:

  • The esterase-like activity of C3 involves a general-base mechanism mediated by a catalytic group X in the C3d region.
  • This catalytic mechanism may also be involved in the formation of acyl ester bonds after the hydrolysis of the internal thiolester bond in native C3.