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- W2050651693 abstract "1. A preparation of ovomucin from chicken egg white was shown to be essentially free of other egg white proteins by starch-gel electrophoresis. It contained 83.3% anhydroamino acids, 2.2% total sulfur, 0.44% sulfate sulfur and 14.2% total nitrogen. The protein portion of ovomucin contained 16.6% nitrogen. The 18.6% carbohydrate consisted of 7.2% hexosamine, 7.4% hexose and 4.0% sialic acid. The amino acid composition is similar to that of ovomucoid. 2. The ovomucin was characterized by free-boundary electrophoresis, ultracentrifugation, by osmotic pressure and viscosity measurements, and by electron microscopy. When disaggregated in 6 M guanidine · HCl plus 0.2 M mercaptoethanol, the resulting glycopeptide chains had a number-average molecular weight of 1.1 · 105 and a viscosity-average molecular weight of 1.6 · 105. 3. Optical rotatory dispersion and circular dichroism measurements indicate that ovomucin has little α-helix content. Both ao and bo show only minor changes with pH or upon addition of mercaptoethanol, although the intrinsic viscosity, a strong function of salt concentration, is markedly decreased by addition of mercaptoethanol. Ovomucin is probably composed of extended glycoprotein chains held together by disulfide cross-links. It appears inherently heterogeneous." @default.
- W2050651693 created "2016-06-24" @default.
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- W2050651693 date "1970-04-01" @default.
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- W2050651693 title "Chemical and physical characterization of ovomucin, a sulfated glycoprotein complex from chicken eggs" @default.
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- W2050651693 doi "https://doi.org/10.1016/0005-2795(70)90151-0" @default.
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