Sequence of membrane-associated thyroid hormone binding protein from bovine liver: its identity with protein disulphide isomerase
K Yamauchi, T Yamamoto, H Hayashi, S Koya… - Biochemical and …, 1987 - Elsevier
K Yamauchi, T Yamamoto, H Hayashi, S Koya, H Takikawa, K Toyoshima, R Horiuchi
Biochemical and biophysical research communications, 1987•ElsevierThe complementary DNAs of the bovine liver membrane-associated 3, 5, 3′-triiodo-L-
thyronine binding protein with 55 k-dalton (T3BP) were cloned and the nucleotide
sequences were determined. Monospecific antibodies against T3BP were used to screen a
bovine liver cDNA library in λgtll. We analyzed the sequences of two cloned T3BP cDNAs.
The clones encoded a polypeptide of 510 amino acid residues, including a signal peptide of
20 amino acid. Northern blot analysis of bovine and human RNA showed that the mRNAs …
thyronine binding protein with 55 k-dalton (T3BP) were cloned and the nucleotide
sequences were determined. Monospecific antibodies against T3BP were used to screen a
bovine liver cDNA library in λgtll. We analyzed the sequences of two cloned T3BP cDNAs.
The clones encoded a polypeptide of 510 amino acid residues, including a signal peptide of
20 amino acid. Northern blot analysis of bovine and human RNA showed that the mRNAs …
Abstract
The complementary DNAs of the bovine liver membrane-associated 3,5,3′-triiodo-L-thyronine binding protein with 55 k-dalton (T3BP) were cloned and the nucleotide sequences were determined. Monospecific antibodies against T3BP were used to screen a bovine liver cDNA library in λgtll. We analyzed the sequences of two cloned T3BP cDNAs. The clones encoded a polypeptide of 510 amino acid residues, including a signal peptide of 20 amino acid. Northern blot analysis of bovine and human RNA showed that the mRNAs encoding T3BP are 2.7 kilobase in length. Amino acid sequence of N-terminal and other three peptides isolated from purified T3BP were found in the predicted amino acid sequence from the cDNA sequence. The predicted amino acid sequence is closely homologous (93%) with that of rat protein disulphide isomerase (EC 5.3.4.1), which catalyzes the isomerization of the protein disulphide bonds and has been shown to play an important role in post-translational regulation. The results suggest that T3BP and protein disulphide isomerase should be the same protein.
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