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Related Experiment Videos

Buffalo plasma fibronectin: a physico-chemical study.

N Ahmed1, R Chandra, H G Raj

  • 1Dr B R Ambedkar Center for Biomedical Research, University of Delhi, India.

Indian Journal of Biochemistry & Biophysics
|May 7, 2002
PubMed
Summary

Buffalo plasma fibronectin (FN) was purified and characterized, revealing properties similar to human plasma FN. This research provides insights into the structure and function of buffalo fibronectin.

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Area of Science:

  • Biochemistry
  • Proteomics
  • Comparative Biology

Background:

  • Plasma fibronectin (FN) is a crucial extracellular matrix glycoprotein involved in various biological processes.
  • Understanding the biochemical properties of FN across different species, like buffalo (Babulis babulis), enhances comparative biological knowledge.

Purpose of the Study:

  • To purify and characterize plasma fibronectin from buffalo.
  • To compare the biochemical and structural properties of buffalo plasma FN with those of human and bovine plasma FN.

Main Methods:

  • Purification using gelatin-Sepharose and heparin-Sepharose affinity chromatography.
  • Analysis of molecular mass via SDS-PAGE.
  • Immunological cross-reactivity assessment using Western blotting.

Related Experiment Videos

  • Determination of amino acid composition, carbohydrate content, and sulfhydryl groups.
  • Structural conformation analysis using physical parameters (Stoke's radius, viscosity) and rotary shadowing electron microscopy.

    • Main Results:

    • Buffalo plasma FN was purified to homogeneity, showing two subunits (246 kDa and 228 kDa).
    • It demonstrated immunological cross-reactivity with anti-human plasma FN and had similar amino acid composition to human and bovine FN.
    • Physical and electron microscopy data indicated an extended, non-globular conformation for buffalo plasma FN.

    Conclusions:

    • Buffalo plasma fibronectin shares significant biochemical and structural similarities with human plasma fibronectin.
    • These findings contribute to the understanding of fibronectin's conserved properties across mammalian species.