Structure and composition of soluble feather keratin

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منابع مشابه

Structure and composition of soluble feather keratin.

Blackburn, S. & Lowther, A. G. (1951). Biochem. J. 48, 126. Bowes, J. H. & Moss, J. A. (1953). Biochem. J. 55, 735. Courts, A. (1954). Biochem. J. 58, 70. Craig, L. C. & Craig, D. (1950). In Technique of Organic Chemistry, vol. 3, chap. 4. Ed. by Weissberger, A. New York: Interscience Publishers, Inc. Craig, L. C. & Post, 0. (1949). Analyt. Chem. 21, 500. Felix, K. (1953). In The Chemical Struc...

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Molecular size, shape and aggregation of soluble feather keratin.

The keratins are epidermal proteins which contain a high percentage of cystine and, in the solid state, can form macroscopic structures in which there is a high degree of order in the arrangement of the polypeptide chains. Because ofthe last characteristic they have been an invaluable material to study the structure of proteins by the diffraction, or scatter, of X-rays. It was considered that m...

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Extrusion of Feather Keratin

Keratin obtained from poultry feathers was extruded at 120°C using a combination of glycerol, water, and sodium sulfite as processing aids. Rheological properties were assessed as a function of water, glycerol, and sodium sulfite content as well as extruder die temperature. The lowest viscosity blends at a constant feather keratin concentration of 60 wt % were found at glycerol concentrations t...

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Thermal behavior of fowl feather keratin.

Differential scanning calorimetry (DSC) was applied to elucidate the thermal behavior of fowl feather keratins (barbs, rachis, and calamus) with different morphological features. The DSC curves exhibited a clear and relatively large endothermic peak at about 110-160 degrees C in the wet condition. A considerable decrease in transition temperature with urea and its helical structure content esti...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1956

ISSN: 0306-3283

DOI: 10.1042/bj0630576