AMINO ACID SEQUENCE OF FEATHER KERATIN FROM FOWL
نویسندگان
چکیده
منابع مشابه
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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The present research was conducted to extract keratin protein from chicken feathers. Protein is an important nutrient needed by our body to maintain body structures and is an important ingredient for cosmetic products. Chicken feathers have high level of keratin protein content and can become a suitable protein source. The main processes involved are first dissolving chicken feathers using diff...
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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...
متن کاملThe amino acid sequence of protein SCMK-B2A from the high-sulphur fraction of wool keratin.
1. The amino acid sequence of protein SCMK-B2A, a reduced and S-carboxymethylated protein from the high-sulphur fraction of wool, has been determined. 2. This protein of 171 amino acid residues displays both a high degree of internal homology and extensive external homology with other members of the SCMK-B2 group of proteins. 3. Evidence is presented which suggests that the SCMK-B2 group of pro...
متن کاملThe amino acid sequence of protein SCMK-B2C from the high-sulphur fraction of wool keratin.
1. The amino acid sequence of a protein from the reduced and carboxymethylated high-sulphur fraction of wool has been determined. 2. The sequence of this S-carboxymethylkerateine (SCMK-B2C) of 151 amino acid residues displays much internal homology and an unusual residue distribution. Thus a ten-residue sequence occurs four times near the N-terminus and five times near the C-terminus with few c...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1983
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1983.tb07390.x