{"refrec":{"BRefID":113518,"RR":"Tsutsui, N.; Ohira, T.; Kawazoe, I.; Takahashi, A.; Wilder, M.N. (2007). Purification of sinus gland peptides having vitellogenesis-inhibiting activity from the whiteleg shrimp Litopenaeus vannamei. Mar. Biotechnol. 9(3): 360-369. https://dx.doi.org/10.1007/s10126-006-6151-0","BEntID":107974,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". Mar. Biotechnol. 9(3): 360-369. https://dx.doi.org/10.1007/s10126-006-6151-0","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Tsutsui, N.; Ohira, T.; Kawazoe, I.; Takahashi, A.; Wilder, M.N.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Tsutsui, N. et al.","Englishabstract":"Vitellogenesis-inhibiting hormone (VIH) in Crustacea belongs to the crustacean hyperglycemic hormone (CHH)-family. To characterize multiple VIH molecules in the whiteleg shrimp Litopenaeus vannamei, seven CHH-family peptides designated as Liv-SGP-A, -B, -C, -D, -E, -F, and -G were purified by reversed-phase HPLC and identified by N-terminal amino acid sequencing. The dose-response effects of these peptides on vitellogenin mRNA levels were examined using in vitro incubation of ovarian fragments of the kuruma prawn Marsupenaeus japonicus. Liv-SGP-D showed no significant inhibitory activities, while the other six peptides significantly reduced vitellogenin mRNA levels, however, with differing efficacies, in the order of Liv-SGP-C, -F, -G > -A, -B > -E. Liv-SGP-G was the most abundant CHH-family peptide in the sinus gland and showed strong vitellogenesis-inhibiting activity. As a result of detailed structural analysis, its complete primary structure was determined; it consisted of 72 amino acid residues and possesses an amidated C-terminus. 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