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

Multiple aggregation factors in cartilage proteoglycan.

J D Gregory

    The Biochemical Journal
    |June 1, 1973
    PubMed
    Summary
    This summary is machine-generated.

    Bovine nasal proteoglycans aggregate via essential linking factors. These factors enable proteoglycan subunit aggregation even after chondroitinase digestion, highlighting their crucial role in cartilage structure.

    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

    Cognitive Behaviour Therapy for Health Anxiety: A Systematic Review and Meta-Analysis - CORRIGENDUM.

    Behavioural and cognitive psychotherapy·2017
    Same author

    Overgeneral autobiographical memory and depression in older adults: a systematic review.

    Aging & mental health·2017
    Same author

    Effect of proteoglycan removal on solute mobility in articular cartilage.

    Journal of biomechanics·1997
    Same author

    Kinetic, binding, and NMR studies of perdeuterated yeast phosphoglycerate kinase and its interactions with substrates.

    Archives of biochemistry and biophysics·1995
    Same author

    Substrate activity of Rh(III)ATP with phosphoglycerate kinase and the role of the metal ion in catalysis.

    Archives of biochemistry and biophysics·1994
    Same author

    Arrangement of substrates at the active site of yeast phosphoglycerate kinase. Effect of sulfate ion.

    The Journal of biological chemistry·1993
    Same journal

    Mechanistic insights into acetylated histone recognition by the CECR2 bromodomain.

    The Biochemical journal·2026
    Same journal

    Nanobodies against Plasmodium adhesins that block receptor engagement and malaria parasite invasion.

    The Biochemical journal·2026
    Same journal

    Persistence without turnover: the RhoG G12E mutant highlights the role of nucleotide cycling in RhoG signaling.

    The Biochemical journal·2026
    Same journal

    Alternative Splicing of Rice Chloroplastic CuZn Superoxide Dismutase, OsCSD2: Impact on expression and protein characteristics.

    The Biochemical journal·2026
    Same journal

    Difference and similarity between the ubiquitous secretory pathway Ca2+-ATPases, SERCA2b, and SPCA1a.

    The Biochemical journal·2026
    Same journal

    A molecular perspective on dimethylarginine dimethylaminohydrolases structure and function.

    The Biochemical journal·2026
    See all related articles

    Area of Science:

    • Biochemistry
    • Biomaterials Science

    Background:

    • Proteoglycans are key components of cartilage extracellular matrix.
    • Bovine nasal septa provide a rich source of proteoglycans for research.

    Purpose of the Study:

    • To investigate the role of linking factors in proteoglycan aggregation.
    • To determine if chondroitinase digestion affects proteoglycan aggregation in the presence of linking factors.

    Main Methods:

    • Isolation and purification of proteoglycans from bovine nasal septa.
    • Separation of proteoglycan subunits and linking factors using CsCl density gradient centrifugation.
    • Enzymatic digestion of purified proteoglycan subunits with chondroitinase.

    Main Results:

    • Proteoglycans from bovine nasal septa exist as partially aggregated complexes containing linking factors.

    Related Experiment Videos

  • Two essential linking factors were identified and separated from proteoglycan subunits.
  • Chondroitinase digestion of proteoglycan subunits did not prevent aggregation when linking factors were present.
  • Conclusions:

    • Linking factors are essential for the aggregation of proteoglycan subunits.
    • The aggregation mechanism mediated by linking factors is independent of the glycosaminoglycan chains susceptible to chondroitinase digestion.