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Paul Russell, Ernst R. Tamm, Franz J. Grehn, Greda Picht, Mark Johnson; The Presence and Properties of Myocilin in the Aqueous Humor. Invest. Ophthalmol. Vis. Sci. 2001;42(5):983-986.
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purpose. To determine whether myocilin is present in the aqueous humor (AH) and
to examine certain properties of this protein.
methods. Human AH was obtained at the time of either glaucoma surgery or
cataract extraction. Monkey AH was obtained at the time of death, and
bovine aqueous was obtained from eyes delivered from an abattoir.
Column chromatography was performed on aqueous samples to determine the
approximate size of the myocilin present. Sodium dodecyl
sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) and western
blot analysis were performed using antibody prepared against a peptide
sequence in myocilin. Analysis of the bovine proteins present in AH
that were retained by a microporous filter was also performed using
western blot analysis.
results. By western blot analysis, myocilin was present in human,
monkey, and bovine AH. The apparent molecular size of the myocilin
present in the AH were greater than 250,000 Da, when quantified with a
gel filtration column. Myocilin appeared to be hydrophobic and was one
of the proteins that was retained on microporous filters that were
obstructed by AH.
conclusions. Myocilin is a constituent in the AH. It appears that myocilin is a
hydrophobic protein that may exist in an oligomeric state or in
association with other proteins. Myocilin is retained by microporous
filters and may be involved in the obstruction of these filters that
occurs when AH is perfused through them.
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