Biochemical studies of the relationship between iodothyronine 5'-monodeiodinase and protein disulphide isomerase in rat liver.
The relationship between type I iodothyronine 5'-monodeiodinase (5'-MD) and protein disulphide isomerase (PDI) was investigated by using a synthetic 18-amino acid peptide (LAP475c), which corresponds to the sequence of amino acids at position 373-390 of PDI including its active site, and anti-LAP475c antibody. Western blot analysis revealed that our anti-LAP475c antibody was highly specific for 57K protein in solubilized rat liver microsomal protein (SRLMP) that corresponded to PDI. Anti-LAP475c IgG (1:100 dilution) precipitated 46% of 5'-MD. These data suggest that PDI may play a regulatory role in the 5'-monodeiodination reaction.
Sakane
S
S
First Department of Medicine, Osaka Medical College, Takatsuki, Japan.
Chopra
I J
IJ
Takamatsu
J
J
Ohsawa
N
N
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D001665:Binding Sites; D015153:Blotting, Western; D015971:Gene Expression Regulation, Enzymologic; D007453:Iodide Peroxidase / Q000737:chemistry / Q000378:metabolism*; D007535:Isomerases / Q000378:metabolism*; D008862:Microsomes, Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D019704:Protein Disulfide-Isomerases; D051381:Rats
D000911:Antibodies, Monoclonal; D007453:Iodide Peroxidase; D007535:Isomerases; D019704:Protein Disulfide-Isomerases