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ECB-ART-43335
Appl Biochem Biotechnol 2014 May 01;1731:143-54. doi: 10.1007/s12010-014-0823-4.
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Purification and characterization of pepsin-solubilized collagen from skin of sea cucumber Holothuria parva.

Adibzadeh N , Aminzadeh S , Jamili S , Karkhane AA , Farrokhi N .


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.

PubMed ID: 24676570
Article link: Appl Biochem Biotechnol


Genes referenced: LOC100887844 LOC100892350 LOC588990 pelp1