Masters Theses
Abstract
"Thyroglobulin was digested with trypsin. An iodotyrosyl-containing peptide was isolated from tryptic digests by a combination of electrophoresis and paper chromatography. The amino acid sequence of this peptide was determined by applying the Edman degradation and by using the proteolytic enzyme, carboxypeptidase A. The sequence of this peptide is: NH₂-Ala-Ile(Leu)-Ala-Ser-Phe-Gly-Asp-Tyr-Glu-Phe-COOH The importance of the position of the tyrosyl residue which is iodinated to form monoiodotyrosine (MIT) , diiodotyrosine (DIT) , and thyroxine (T₄) is considered in connection with the structure-activity relationship of the protein"--Abstract, page ii.
Advisor(s)
Nicholson, Larry M.
Committee Member(s)
Gale, Nord L.
Siehr, Donald J.
Department(s)
Chemistry
Degree Name
M.S. in Chemistry
Publisher
University of Missouri--Rolla
Publication Date
1970
Pagination
viii, 49 pages
Note about bibliography
Includes bibliographical references (pages 75-77).
Rights
© 1970 Pai-Chun Chiang, All rights reserved.
Document Type
Thesis - Open Access
File Type
text
Language
English
Subject Headings
Amino acid sequence
Amino acids -- Analysis
Peptides -- Analysis
Thesis Number
T 2468
Print OCLC #
6028237
Electronic OCLC #
864828876
Link to Catalog Record
Recommended Citation
Chiang, Pai-Chun, "Amino acid sequence of an iodotyrosyl-containing peptide produced by tryptic digestion of thyroglobulin" (1970). Masters Theses. 7150.
https://scholarsmine.mst.edu/masters_theses/7150
