Intron sequences modulate feather keratin gene transcription inXenopusoocytes

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...

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...

Tiie Structiure of Feather Raciiis Keratin

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...

Regulation of a human epidermal keratin gene: sequences and nuclear factors involved in keratinocyte-specific transcription.

The keratinocyte is a major cell type of the body, and in epidermis, keratinocytes have potential for future gene targeting and drug therapy. Despite the importance of keratinocytes in cell biology and medicine, little is known about the molecular mechanisms underlying keratinocyte-specific gene expression. Here, we report the first detailed characterization of the sequences and factors control...