Sulfhydryl Oxidase from Egg White

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Isolation and characterization of sulfhydryl oxidase from bovine milk.

A method is described for purification of sulfhydryl oxidase from bovine milk which consistently yields preparations with greater than 3000-fold purification over skim milk. A concentration-dependent association-dissociation of the enzyme was adapted to the development of an isolation procedure. Purified preparations exhibited two zones, both of which displayed activity, upon polyacrylamide dis...

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Sulfhydryl Groups in Films of Egg Albumin

1. The same number of SH groups reduces ferricyanide in surface films of egg albumin as in albumin denatured by urea, guanidine hydrochloride, Duponol, or heat, provided the ferricyanide reacts with films while they still are at the surface and with the denatured proteins while the denaturing agent (urea, heat, etc.) is present. 2. The SH groups of a suspension of egg albumin made by clumping t...

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The Sulfhydryl Groups of Egg Albumin

1. 1 cc. of 0.001 M ferricyanide, tetrathionate, or p-chloromercuribenzoate is required to abolish the SH groups of 10 mg. of denatured egg albumin in guanidine hydrochloride or Duponol PC solution. Both the nitroprusside test and the ferricyanide reduction test are used to show that the SH groups have been abolished. 2. 1 cc. of 0.001 M ferrocyanide is formed when ferricyanide is added to 10 m...

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Native and denatured egg white protein IgE tests discriminate hen's egg allergic from egg-tolerant children.

BACKGROUND Accurate diagnosis of egg allergy by IgE testing is challenged by a large number of atopic subjects sensitized, but clinically tolerant to eggs. In addition, discrimination between allergy to raw only, or raw and cooked egg allergy is important. In this study, we investigate the diagnostic performance of IgE tests to native and denatured egg proteins. METHODS According to food chal...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1999

ISSN: 0021-9258

DOI: 10.1074/jbc.274.32.22147