Abstract
We have isolated and determined the nucleotide sequence of overlapping cDNA clones, representing the entire structural gene for pig thyroid peroxidase. The protein coding region extends from an ATG residue at base 252 to a termination codon at base 3030, coding for a 100.4-kDa apoprotein of 926 amino acids. The derived amino acid composition agrees well with the experimentally determined amino acid composition of purified pig thyroid peroxidase. Five potential glycosylation sites are present in the protein. Potential membrane spanning regions are present at the amino-terminal end (1-23) and near the carboxyl-terminal end (845-870) of the protein. These data indicate that pig thyroid peroxidase is synthesized as a single polypeptide that is membrane-bound.
Highlights
Francisco, California 94121, the University of California, San Francisco, Cclifornia 94143, and the $Department of Pharmacology, University of Texas Health Science Center, Dallas, Texas 75235 moto’s thyroiditis is, at least in part, human thyroid peroxidase (5)
We have recently reported the isolation and characterization of a cDNA clone for porcine thyroid peroxidase (8).This cloning was accomplished by means of screening a porcine thyroid cDNA Xgtll library with oligonucleotide probes synthesized on the basis of the amino acid sequence of tryptic fragments of highly purified porcine thyroid peroxidase
In the present report we describe the full-length nucleotide and primary amino acid sequence of porcine thyroid peroxidase
Summary
From the $Department of Medicine, Metabolism Section (I 1 IF), Veterans’ Administration Medical Center, San. In the present report we describe the full-length nucleotide and primary amino acid sequence of porcine thyroid peroxidase. Five potential glyco- lecular Biology Resource Center) for use as primers in the sequencing technique to avoid the necessity for restriction digestion and subclonsylation sites are present in the protein. Amino acid composition of purified pig thyroid (845-870) of the protein These data indicate that pig peroxidase was performed by Dr Craig Miles at theNational Jewish thyroid peroxidaseis synthesized as a single polypep- Center for Immunology and Respiratory Medicine, Denver, CO. Similar purification of human thyroid peroxidase has indicated two forms of the enzyme of 100 and 107 kDa (4). The nucleotide sequence(s)reported in this paper has been submitted to the GenBankTM/EMBLData Bank with accession number(s)
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