دورية أكاديمية
Expression of a functional thyroglobulin fragment in a baculovirus system.
| العنوان: | Expression of a functional thyroglobulin fragment in a baculovirus system. |
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| المؤلفون: | den Hartog MT; Department of Endocrinology, University of Amsterdam, The Netherlands., Sijmons CC, Kristel PM, Bakker O, de Vijlder JJ |
| المصدر: | Journal of molecular endocrinology [J Mol Endocrinol] 1993 Oct; Vol. 11 (2), pp. 161-6. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: BioScientifica Country of Publication: England NLM ID: 8902617 Publication Model: Print Cited Medium: Print ISSN: 0952-5041 (Print) Linking ISSN: 09525041 NLM ISO Abbreviation: J Mol Endocrinol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Jan. 2011- : Bristol, UK : BioScientifica Original Publication: Bristol, U.K. : Journal of Endocrinology, Ltd., c1988- |
| مواضيع طبية MeSH: | Nucleopolyhedroviruses/*genetics , Recombinant Fusion Proteins/*biosynthesis , Thyroglobulin/*biosynthesis, Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA, Complementary/genetics ; Gene Expression Regulation, Viral ; Iodine/metabolism ; Lactoperoxidase/metabolism ; Molecular Sequence Data ; Moths ; Polymerase Chain Reaction ; Protein Processing, Post-Translational ; Recombinant Fusion Proteins/genetics ; Thyroglobulin/genetics ; Thyroxine/biosynthesis |
| مستخلص: | The synthesis is described of an N-terminal thyroglobulin (Tg) polypeptide of 27 kDa, which is capable of hormonogenesis, in a baculovirus system. This polypeptide was made using a 657 bp Tg cDNA cloned from human thyroid RNA by a polymerase chain reaction method. The cDNA contained the information for the Tg signal peptide, the N-terminally located site for thyroid hormone formation and, at the 3' end, a sequence coding for six histidine residues. The fragments produced were purified using a nickel-nitrilotriacetic acid column using these six histidine residues. The products were analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and showed two glycosylated fragments of 32 and 34 kDa, both of which started with asparagine. Iodination of the fragments with lactoperoxidase in vitro resulted in the formation of thyroxine (T4). The formation rate of T4 in the fragments was about five times lower than that of the mature Tg dimer of 660 kDa, but ten times more rapid than in bovine serum albumin under the same conditions. |
| المشرفين على المادة: | 0 (DNA, Complementary) 0 (Recombinant Fusion Proteins) 9010-34-8 (Thyroglobulin) 9679TC07X4 (Iodine) EC 1.11.1.- (Lactoperoxidase) Q51BO43MG4 (Thyroxine) |
| تواريخ الأحداث: | Date Created: 19931001 Date Completed: 19940304 Latest Revision: 20191210 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1677/jme.0.0110161 |
| PMID: | 8297472 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0952-5041 |
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| DOI: | 10.1677/jme.0.0110161 |