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41.
To investigate the tissue-specificities of isozymes and the genetic structure of wild spotted halibut ( Verasper variegatus) population, horizontal starch gel electrophoresis was performed on 45 individuals collected in part of the Yellow Sea. The performances of 17 isozymes in 8 kinds of tissues or organs were screened preliminarily in a TC-7.0 buffer system. The results showed that the screened isozymes displayed remarkable tissue-specificities. Finally, 14 enzymes (AAT, ADH, EST, GPI, G3PDH, IDHP, LAP, LDH, MDH, MPI, PGDH, PGM, SDH and SOD) and 4 kinds of tissues (eye, skeleton muscle, liver and heart) were selected for genetic analysis. Fourteen isozymes are encoded by 20 loci, and 9 of them are poly-morphic. The polymorphic loci are AAT-1*, GPI-2*, G3PDH*, IDHP-1*, LDH*, MPI*, PGM-1*, PGM-2* and SDH*, and the proportion of polymorphic loci is 0.450 0 (P0.99). The mean values of observed and expected heterozygosities are 0.027 8 and 0.026 5, respectively and the average effective number of alleles is 1.067 5.  相似文献   
42.
A full-length cDNA encoding translationally controlled tumor protein of marine flatfish turbot (Scophthalmus maximus), SmTCTP, was isolated with rapid amplification of cDNA Ends (RACE). SmTCTP consisted of a 5' untranslated region (UTR) of 84 bp, a 3' UTR of 451 bp and an open reading flame (ORF) of 513 bp, encoding a protein of 170 amino acid residues, which contained two signature sequences of TCTP family. The 5'UTR of SmTCTP started with a 5'-terminal oligopyrimidine tract (5'-TOP), a typical feature for translationaily controlled mRNAs. The deduced amino acid sequence of SmTCTP was similar to the other known verte-brate TCTPs in a range of 58.8% to 64.1%. The length offish TCTPs was diverse among species, e.g., TCTP of turbot and sea perch (Lateolabrax japonicus) is 170 aa in length, while that of zebrafish (Danio rer/o) and rohu (Labeo rohita) is 171 aa in length. North-ern blot analysis revealed that SmTCTP has only one type of mRNA. Its expression level in albino skin was slightly higher than that in normal skin. We constructed the pET3Oa-SmTCTP expression plasmid. The recombinant protein of His-tag SmTCTP was over-expressed in E. coli, purified and identified with peptide mass fingerprinting. These results may pave the way of further inves-tigation of the biological function of TCTP in fish.  相似文献   
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