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

M Richard1, R Letoublon, P Louisot

  • 1Laboratoire de Chimie Biologique, Faculté de Médecine, 69, Lyon, France

FEBS Letters
|January 26, 1970
PubMed
Summary
This summary is machine-generated.

Aspergillus oryzae microsomes transfer mannose to proteins from GDP-mannose. This mannose transfer activity is specific to microsomes, with all transferred mannose confirmed after acid hydrolysis.

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

Correlations between clinical motor scores and CMAP in patients with type 2 spinal muscular amyotrophy treated with nusinersen.

Archives de pediatrie : organe officiel de la Societe francaise de pediatrie·2023
Same author

Validation of quantitative real-time polymerase chain reaction for detection of Legionella pneumophila in hospital water networks.

The Journal of hospital infection·2023
Same author

[Acute dyspnea in a 49 year-old man].

La Revue de medecine interne·2022
Same author

Identification of TB space-time clusters and hotspots in Ouest <i>département</i>, Haiti, 2011-2016.

Public health action·2021
Same author

Introducing new and repurposed TB drugs: the endTB experience.

The international journal of tuberculosis and lung disease : the official journal of the International Union against Tuberculosis and Lung Disease·2020
Same author

Producing three-dimensional printed models of the hepatobiliary system from computed tomography imaging data.

Annals of the Royal College of Surgeons of England·2020
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
Same journal

Overlapping gut microbiome signatures in aging and disease are characterized by enrichment of medication-associated oral microbes in the gut.

FEBS letters·2026
Same journal

Csk binding to integrin β3 is regulated by tyrosine and threonine phosphorylation of β3.

FEBS letters·2026
Same journal

Mixed-class J-domain protein scaffolds promote expanded aggregate handling and multivalent Hsp70 engagement during functional disaggregase assembly.

FEBS letters·2026
See all related articles

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Understanding protein glycosylation in fungi is crucial for various biotechnological applications.
  • Aspergillus oryzae is a key organism in food fermentation and enzyme production.
  • The initial steps of mannosylation involve the transfer of mannose residues to protein acceptors.

Purpose of the Study:

  • To investigate the subcellular localization of mannose transfer activity in Aspergillus oryzae.
  • To identify the specific fraction responsible for transferring mannose from GDP-mannose to protein acceptors.
  • To characterize the nature of the transferred mannose.

Main Methods:

  • Preparation of smooth microsomal fractions from Aspergillus oryzae.
  • Assay of mannose transfer from GDP-mannose to endogenous protein acceptors in various subcellular fractions.

Related Experiment Videos

  • Acid hydrolysis of labeled microsomal fractions followed by chromatography to identify the transferred sugar.

    • Main Results:

    • Smooth microsomal fractions from Aspergillus oryzae demonstrated the ability to transfer mannose from GDP-mannose to endogenous protein acceptors.
    • Mannose transfer activity was exclusively localized to the microsomal fraction among all tested subcellular fractions.
    • Chromatographic analysis confirmed that the transferred radioactive material co-eluted with mannose after acid hydrolysis.

    Conclusions:

    • The microsomes of Aspergillus oryzae are the primary site for the transfer of mannose to protein acceptors.
    • This enzymatic activity is a key step in the early stages of protein glycosylation in this fungus.
    • The study confirms the direct transfer of mannose moieties, not other mannose-containing compounds.