| Literature DB >> 24676570 |
Nasim Adibzadeh1, Saeed Aminzadeh, Shahla Jamili, Ali Asghar Karkhane, Naser Farrokhi.
Abstract
Pepsin-solubilized collagen (PSC) was extracted from the skin of sea cucumber Holothuria parva and was fractionally characterized. The PSC from H. parva skin consisted of three α1 chains (α1)3, in contrast to calf skin collagen type I with two α1 and one α2 chains (α1)2α2 with approximately 130 kDa each. The maximum transition (Tm) and denaturation temperature (Td) of PSC were determined to be 46.94 and 32.5 °C, respectively. The amino acid composition analysis revealed that glycine, proline, alanine, and hydroxyproline were the abundant amino acids available in extracted PSC. The results showed that the isolated collagen from H. parva has some similar characteristics to previously reported collagens used in food and pharmaceutical industries.Entities:
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Year: 2014 PMID: 24676570 DOI: 10.1007/s12010-014-0823-4
Source DB: PubMed Journal: Appl Biochem Biotechnol ISSN: 0273-2289 Impact factor: 2.926