| Description |
x, 67 leaves : illustrations, photographs ; 29 cm |
| Summary |
"Two iodopeptides were isolated from thyroglobulin that had been digested with trypsin by paper electrophoresis and paper chromatography. The amino acid analysis demonstrated that the amino acid compositions were similar. The N-terminal amino acid of both iodopeptides was shown to be leucine. The amino acid sequence of one of the iodopeptides was determined by the Edman degradation method and digestion with the enzyme Carboxypeptidase A. The sequence was shown to be: NHâ‚‚-Leu-Asn-Ala-Ser-Glu-MIT-Gly-Thr-Ser-Gly-COOH. Other workers have shown that synthetic tyrosyl peptides with the sequence Glu-Tyr are iodinated by the thyroid peroxidase enzyme with a greater specificity than other tyrosyl peptides. This specificity would seem to indicate that the glutamic acid residues act as a recognition site for the thyroid peroxidase enzyme in the iodination of the tyrosine residues"--Abstract, leaf ii. |
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