Masters Theses

Abstract

"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: NH₂-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, page ii.

Advisor(s)

Nicholson, Larry M.

Committee Member(s)

Siehr, Donald J.
Grigoropoulos, Sotirios G.

Department(s)

Chemistry

Degree Name

M.S. in Chemistry

Publisher

University of Missouri--Rolla

Publication Date

1974

Pagination

x, 67 pages

Note about bibliography

Includes bibliographical references (pages 64-66).

Rights

© 1974 Frederick E. Bishop, Jr., All rights reserved.

Document Type

Thesis - Restricted Access

File Type

text

Language

English

Library of Congress Subject Headings

Peptides -- Analysis
Thyroglobulin
Amino acid sequence

Thesis Number

T 2966

Print OCLC #

6023903

Electronic OCLC #

911402614

Link to Catalog Record

Electronic access to the full-text of this document is restricted to Missouri S&T users. Otherwise, request this publication directly from Missouri S&T Library or contact your local library.

http://laurel.lso.missouri.edu/record=b1066912~S5

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