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PMID: 6159926 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Restriction mapping of synthetic thyroglobulin structural gene as a means of investigating thyroglobulin structure.

Biochimica et biophysica acta ·Vol. 610 ·No. 1 ·1980-11-14 ·Pages 189-94

Vassart G, Brocas H

Abstract

Bovine 33 S thyroglobulin mRNA was reverse transcribed into double-stranded DNA under conditions allowing the synthesis of a complete 8 kilobase pair copy. A physical map of the resulting synthetic thyroglobulin structural gene was constructed using six restriction endonucleases. The following conclusions could be drawn: (i) the polypeptide chains in thyroglobulin subunits are identical; (ii) thyroglobulin is composed of a major class of molecules sharing the same primary structure; (iii) there is no evidence for precise internal repetition in the structure of thyroglobulin subunits.

MeSH Terms
Animals Base Composition Base Sequence Cattle DNA/metabolism DNA Restriction Enzymes Genes Molecular Weight RNA, Messenger/metabolism RNA-Directed DNA Polymerase Thyroglobulin/biosynthesis
Chemicals
RNA, Messenger DNA Thyroglobulin RNA-Directed DNA Polymerase DNA Restriction Enzymes
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Vassart G
Brocas H
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1980-11-14
Pages
189-94
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
Grants
NIADDK NIH HHS · AM 21732 · United States
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