NDLI: Purification and characterization of hatching enzyme from flounder Paralichthys olivaceus

Content Provider	Springer Nature Link
Author	Shi, Zhen Ping Fan, Ting Jun Cong, Ri Shan Wang, Xiao Feng Sun, Wen Jie Yang, Ling Ling
Copyright Year	2006
Abstract	Using chorion of Paralichthys as a specific substrate, hatching enzyme (HE) from Paralichthys olivaceus (PHE) was purified by gel-filtration and ion-exchange chromatography, and characterized in terms of its molecular weight and enzymatic properties in this study. It was found that the molecular size of PHE is about 34.8 kDa in SDS-PAGE. The PHE had obvious choriolytic activity, which was optimal at pH 7.0 and temperature of 35 °C, respectively. The Km value of the PHE for casein was 4.28 mg ml−. The PHE was very sensitive to trypsin-specific inhibitors, especially serine protease-specific inhibitors, such as LBTI, SBTI, bestatin and p-APMSF, leupeptin, ovomucoid, PMSF, pepstatin A and TLCK, indicates that it is a trypsin-type serine protease. The PHE was also extremely sensitive to Cu2+ and Ca2+, combined with the results that it was inhibited by EDTA in a dose-dependent manner, indicates this PHE is also a kind of metalloprotease.
Starting Page	35
Ending Page	42
Page Count	8
File Format	PDF
ISSN	09201742
Journal	Fish Physiology and Biochemistry
Volume Number	32
Issue Number	1
e-ISSN	15735168
Language	English
Publisher	Springer Netherlands
Publisher Date	2006-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	choriolytic activity hatching enzyme metalloprotease Paralichthys olivaceus trypsin-type serine protease Freshwater & Marine Ecology Animal Physiology Animal Anatomy / Morphology / Histology Animal Biochemistry Zoology
Content Type	Text
Resource Type	Article
Subject	Physiology Medicine Biochemistry Aquatic Science

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