NDLI: Purification and identification of a clotting protein from the hemolymph of Chinese shrimp (Fenneropenaeus chinensis)

Content Provider	Springer Nature Link
Author	Wang, Baojie Peng, Hongni Liu, Mei Jiang, Keyong Zhang, Guofan Wang, Lei
Copyright Year	2013
Abstract	The clotting protein (CP) plays important and diverse roles in crustaceans, such as coagulation and lipid transportation. A clotting protein was purified from the hemolymph of Chinese shrimp Fenneropenaeus chinensis (named as Fc-CP) with Q sepharose HP anion-exchange chromatography and phenyl sepharose HP hydrophobic interaction chromatography. Fc-CP was able to form stable clots in vitro in the presence of hemocyte lysate and Ca$^{2+}$, suggesting that the clotting reaction is catalyzed by a Ca$^{2+}$-dependent transglutaminase in shrimp hemocytes. The molecular mass of Fc-CP was 380 kDa under non-reducing conditions and 190 kDa under reducing conditions as was determined with SDS-PAGE. CP exists as disulfide-linked homodimers and oligomers. The N-terminal amino acid sequence of Fc-CP was identical to that of shrimps including Penaeus monodon, Farfantepenaeus paulensis and Litopenaeus vannamei; and similar to that of other decapods. The purified Fc-CP was digested with trypsin and verified on an ABI 4700 matrix-assisted laser desorption/ionization tandem time-of-flight (MALDI-TOF/TOF) mass spectrometry. Our results will aid to better understanding the coagulation mechanism of shrimp hemolymph.
Starting Page	477
Ending Page	483
Page Count	7
File Format	PDF
ISSN	16725182
Journal	Journal of Ocean University of China
Volume Number	12
Issue Number	3
e-ISSN	19935021
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2013-07-25
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Fenneropenaeus chinensis clotting protein purification proteomic identification MALDI-TOF/TOF MS Oceanography Meteorology
Content Type	Text
Resource Type	Article
Subject	Oceanography Ocean Engineering

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