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E. I. ANDERSON; Proteolytic Activity of Bovine Corneal Epithelial Extracts. Invest. Ophthalmol. Vis. Sci. 1967;6(4):348-355.
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Proteolysis of both endogenous and exogenous substrates by the dialyzed soluble fraction of bovine corneal epithelium has been studied. Such variables as pH, temperature, and cation supplementation were chosen to simulate conditions as they may prevail during mechanical or thermal wounding. Endogenous proteolysis at physiologic pH and temperature is stimulated in decreasing order by Mn2+, Mg2+, and Ca2+ at optimal concentrations of 10mM. At 50° C. the optimal concentrations of each cation is reduced to 2 mM. and Ca2+ stimulation is markedly enhanced. The monovalent cations, and especially Na+, critically influence activity. Inhibition or activation of proteolysis by Na+ appears to depend on the extent to which protein configurations are altered. The respective alkaline pH optima for unsupplemented and Mg2+ stimulated proteolysis at 37.5° C. is 8.0 and 8.5. Soybean trypsin inhibitor has essentially no effect on proteolysis, and the Na+ in sodium salicylate accounts for all but 7 per cent of the inhibition observable with this compound.
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