Abstract
Abstract Alpha and beta collagen subunits were isolated from golden pompano skins by cellulose column at different pH. As a result, the α1 subunit and β subunit were successively eluted by a linear gradient of 0–35 mM NaCl at pH 4.7, while α2-subunit was eluted at pH 5.2. SDS-PAGE result showed that the molecular weights of α1, α2 and β subunits were about 131, 119 and 256 kDa, respectively. The contents of glycine, alanine and imino acids in the α1 subunit were more similar to the β subunit than α2 subunit. Analyses of deduced amino acid sequences revealed that the theoretical sizes and isoelectric points of collagen α1 were 137 kDa and pH 5.95, while those of collagen α2 were 126 kDa and pH 9.27, respectively. Compared to the collagen α2, collagen α1 had a cysteine-rich domain, more tripeptide unit of Gly-Pro-Pro, and specific α-helix domain.
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