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Electrophoretic and morphologic studies on normal human white matter obtained at surgery with special reference to

K A Ansari, H Hendrickson, A Rand

    Journal of Neuropathology and Experimental Neurology
    |November 1, 1976
    PubMed
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    Normal human white matter basic protein is stable and resistant to degradation. Studies using electrophoresis and electron microscopy show it remains unaffected by incubation, even after 18 hours at room temperature.

    Area of Science:

    • Neuroscience
    • Biochemistry

    Background:

    • Human white matter contains basic proteins crucial for myelin structure.
    • Understanding the stability of these proteins is important for neurological research and diagnostics.

    Purpose of the Study:

    • To investigate the stability and potential degradation of basic protein in normal human white matter.
    • To correlate electrophoretic and electron microscopic findings regarding protein integrity.

    Main Methods:

    • Acrylamide disc gel electrophoresis of human white matter homogenates.
    • Incubation of white matter samples at different temperatures (4°C and 23°C) for up to 18 hours.
    • Electron microscopy of incubated white matter samples.

    Main Results:

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  • The basic protein band in white matter homogenates showed no degradation after incubation at 23°C for 18 hours.
  • Electron microscopy revealed minor lamellar separation in incubated samples, less severe than post-mortem changes.
  • Findings support the location of basic protein on the cytoplasmic surface of myelin lamellae.

    • Conclusions:

    • Basic protein in fresh human white matter exhibits significant resistance to autolytic degradation in vitro.
    • These findings corroborate previous studies on post-mortem white matter.
    • The stability of basic protein has implications for understanding white matter pathology and preservation.