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ECB-ART-45060
Springerplus 2016 Nov 03;51:1998. doi: 10.1186/s40064-016-3484-7.
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Characterization of a novel hatching enzyme purified from starfish Asterina pectinifera.

Choi JH , Kim SM .


Abstract
Hatching enzyme is a protease which can degrade the membrane of egg. In this study, a hatching enzyme was purified from starfish (Asterina pectinifera) with 6.34 fold of purification rate, 5.04 % of yield, and 73.87 U/mg of specific activity. The molecular weight of starfish hatching enzyme was 86 kDa, which was reduced to 62 kDa after removal of N-linked oligosaccharides. The optimal pH and temperature of the hatching enzyme activity were pH 7.0 and 40 °C, respectively, while those of stability were pH 8 and 20 °C. The kinetic parameters, V max , K m , K cat and K cat /K m values were 0.197 U/ml, 0.289 mg/ml, 112.57 s-1, and 389.52 ml/mg s, respectively. Zn2+ increased the enzyme activity by 167.28 %, while EDTA, TPCK, TGCK, leupeptin, PMSF, and TLCK decreased. In addition, Ca2+, Mg2+, and Cu2+ did not affect the enzyme activity. The starfish hatching enzyme activity pretreated with EDTA was recovered by Zn2+. Therefore, the starfish hatching enzyme was classified as a serine-zinc protease.

PubMed ID: 27933254
PMC ID: PMC5120168
Article link: Springerplus


Genes referenced: LOC100888042 LOC105438433 LOC594261 LOC752081 LOC756768 mmp7 ngly1


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References [+] :
Ala-Kokko, Collagen gene expression in keloids: analysis of collagen metabolism and type I, III, IV, and V procollagen mRNAs in keloid tissue and keloid fibroblast cultures. 1987, Pubmed