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- 저자 : Jiingjau (검색결과 2 건)
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Huh, Tae Lin,PARK, HEE SUNG,Jeng, Jiingjau,Kim, Young Ou,Oh, II Ung,Song, Byoung J. 경북대학교 유전공학연구소 1995 遺傳工學硏究所報 Vol.10 No.1
A 0.6 kb cDNA fragment encoding the human NAD^+-specific isocitrate dehydrogenase α-subunit (H-IDHα) was amplified by PCR using oligonucleotide primers synthesized on the basis of pig tryptic peptide sequences [Huang and Colman (1990) Biochemistry 29, 8266-8273]. With the amplified cDNA as a probe, cDNA clones for IDHα were isolated from a human heart λgt11 cDNA library. The deduced protein sequence of the largest cDNA clone (2628 bp) rendered a precursor protein of 366 amino acids (39591 Da) and a mature protein of 339 amino acids (36640 Da). The deduced H-IDHα protein sequence is highly similar to the partial peptide sequences of the pig enzyme. It is 55, 43 and 44 % identical with yeast NAD^+-specific IDH2, yeast NAD^+-specific IDH1 and monkey NAD^+-specific IDH γ-subunit (IDHγ) respectively. However, it has less similarity (about 30%) to NADP^+-specific IDH from Escherichia coli and bovine mitochondria. These results indicate that the structure of IDHα closely resembles that of IDH2, the catalytic subunit of the yeast enzyme. Structural analysis of the deduced H-IDHα protein revealed that the amino acids responsible for the binding of isocitrate, Mg^(2+) and NAD^+ are highly conserved. It also has two conserved motifs for the binding sites of ATP and ADP, but a canonical Ca^(2+)-binding motif was not recognized. Unusual penta- (ATTTA) and tri-(TAA or ATT) nucleotides which are respectively believed to interact with RNA-binding proteins and be near the endonuclease cleavage sites were frequently recognized in its 3' untranslated region, indicating the possibility of an additional method of regulation of this enzyme. Northern-blot analysis suggests that one mRNA transcript (2.8 kb) exists in cultured HeLa cells. Genomic DNA Southern-blot analysis indicates that the IDHα gene is not closely related to that of the other IDH isoenzymes, and IDHα appears to be encoded by a single gene.
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KIM, SUNG MIN F,Kim, Byung Moon,Jeng, Jiingjau,Soh, Yun jo,Bak, Choong Il,Huh, Jae Wook,Song, Byoung J 생화학분자생물학회 1980 BMB Reports Vol.29 No.2
A 2.1 kb cDNA clone for rat transketolase was isolated from rat liver λgt11 cDNA library and its sequence was determined. The predicted rat transketolase (655 amino acids with M_r 71,186) is highly similar (92%) to that of the human enzyme except that it contains an extra 32 amino acids at its N-terminus. Although it is less similar ($lt;27%) to transketolases from non-mammalian species, the functional motifs such as the catalytic sites and thiamine binding domain are well conserved in the rat enzyme. Southern blot analysis of genomic DNA verified that transketolase appears to be derived from a single gene. Immunoblot and Northern blot analyses suggested that hepatic transketolase was activated pretranslationally by a 2.1fold while little change was observed in brain enzyme, indicating a tissue-specific pretranslational activation during postnatal development.
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