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Sequence of Membrane-Associated Thyroid Hormone Binding Protein From Bovine Liver: Its Identity With Protein Disulphide Isomerase

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, H Takikawa, K Toyoshima, R Horiuchi

Biochem Biophys Res Commun. 1987 Aug 14;146(3):1485-92.

PMID: 3619939

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 lambda gtll. 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP37318493	Protein Disulfide Isomerase from bovine liver		37318-49-3	Price

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