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Effect of GnRH administration on egg production, hormonal and biochemical profile and ovarian histomorphology of spent naked neck layers. [PDF]

open access: yesPoult Sci
Khan S   +8 more
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Inactivation of Complement by Egg Albumin-Rabbit Antiegg Albumin

The Journal of Immunology, 1958
Summary Possible reasons for differences in the degree of inactivation of guinea pig, human, and pig C′ by a fixed quantity of an antigen-antibody system were investigated. It was found that a relatively high concentration of inhibitors in pig serum could account for the absence of fixation of pig C′ by small quantities of antigen ...
G, CAVALLO   +2 more
openaire   +2 more sources

Holograms with egg albumin

SPIE Proceedings, 2008
Two components of the egg as the albumen and their proteins are used for holographic recorded applying lithography technique. This matrix was composed by albumen-glucose and by protein-glucose. The results obtained for the parameter diffraction efficiency with our matrix albumen-glucose was it from 44.1% and for the matrix protein-glucose were two ...
P. Pérez-Salinas   +6 more
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Adsorbed monolayers of egg albumin

Archives of Biochemistry and Biophysics, 1957
Abstract 1. 1. The minimum free energy of adsorption of egg albumin on Pyrex glass at pH 4.66 and at 30 ° is −6829 cal./mole. 2. 2. The force-area curve for egg albumin shows the adsorbed film to be more compact than at an air-water surface. 3. 3.
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Egg albumin microspheres containing sulphamethizole

Journal of Microencapsulation, 1984
Egg albumin microspheres containing sulphamethizole have been prepared by a capillary extrusion procedure. The microspheres were coarse (dvn = 1835 microns) with a narrow size distribution and tended to lose their spherical shape on drying. Scanning electron microscopy revealed that the microspheres were porous with drug concentrated at the periphery ...
M R, Brophy, P B, Deasy
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Agitated egg albumin

Journal of Chemical Education, 1975
Beaten egg white will liquefy and mix readily with water if left to stand at room temperature for several hours.
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Titration of heat-denatured egg albumin

Archives of Biochemistry and Biophysics, 1965
Abstract The titration of native and heat-denatured egg albumin has been compared at a number of ionic strengths. The change of pH of the protein solutions as a function of time at elevated temperatures as well as a function of temperature has been studied. Heat denaturation, acid to pH 7.25, greatly increases the affinity of the protein for hydrogen
H B, BULL, R L, ANTRIM, K, BREESE
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