Soluble egg shell membrane protein as a regulating material for collagen matrix reconstruction.
Soluble egg shell membrane protein (SEP) was prepared from egg shell membrane by the combined treatment of performic acid oxidation (4 or 25 degrees C for 24 h) and pepsin digestion (25 degrees C for 24-72 h) before dialyzing against water and lyophilizing. The yield of SEP was about 16-39%. SEP had high contents of acidic amino acids (320-340 residues/1000 residues) containing cysteic acid (101-108 residues) converted from cystine, a small amount of saccharides, a main molecular weight of 12,000-22,000 and pI 4.2-4.8. SEP accelerated the reconstruction of collagen matrix with ordered molecular rearrangement and reduced redissolution of the collagen matrix under several solvent conditions. SEP elevated the denaturation temperature of the matrix.
Takahashi
K
K
Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Japan.
Shirai
K
K
Kitamura
M
M
Hattori
M
M
D000596:Amino Acids / Q000032:analysis; D003094:Collagen / Q000187:drug effects*; D004220:Disulfides / Q000737:chemistry; D004527:Egg Proteins / Q000494:pharmacology*; D005561:Formates; D008565:Membrane Proteins / Q000494:pharmacology*; D010084:Oxidation-Reduction; D010434:Pepsin A; D011489:Protein Denaturation; D012995:Solubility
D000596:Amino Acids; D004220:Disulfides; D004527:Egg Proteins; D005561:Formates; D008565:Membrane Proteins; C008817:peroxyformic acid; D003094:Collagen; D010434:Pepsin A