Document Detail


Structural Identification and Proteolytic Effects of the Hatching Enzyme from Starfish Asterias Amurensis.
MedLine Citation:
PMID:  24559163     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Hatching enzyme (HE) is secreted from the blastula stage during fertilization and can cleave the egg membrane. The structural identification and proteolytic effects on the collagen and fibrinogen were investigated in this study. Approximate 20 kDa of Asn-linked oligosaccharides were attached to the HE. Five peptide fragments of the starfish HE were homogenous to those of the coat matrix protein of starfish Patiria pectinifera. Amino acids of the starfish HE consisted of mainly Leu (10.0%), Asp (12.5%), and Glu (12.8%). Collagenolytic and fibrinolytic activities of the starfish HE were weaker than those of collagenase and α-chymotrypsin. The degree values of hydrolysis for collagenase and α-chymotrypsin were significantly higher than those of HE in a dose- and time-dependent manner. The peptide mappings of the starfish HE on the collagenolysis (110.7, 84.7, and 20.8 kDa) and fibrinogenolysis (34, 30, and 29 kDa) were different from those of collagenase and α-chymotrypsin. Based on the proteolytic effects on the collagen and fibrinogen, the starfish hatching enzyme might have the potential application to remove the matrix composition in scar or keloid tissue.
Authors:
Zhi Jiang Li; Sang Moo Kim
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-2-21
Journal Detail:
Title:  Protein and peptide letters     Volume:  -     ISSN:  1875-5305     ISO Abbreviation:  Protein Pept. Lett.     Publication Date:  2014 Feb 
Date Detail:
Created Date:  2014-2-24     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9441434     Medline TA:  Protein Pept Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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