Human thyroid-stimulating hormone: structure-function analysis.
This article provides the reader with an overview of methodological strategies to investigate structure-function relationships of human thyroid-stimulating hormone (hTSH). Various aspects of hTSH production, purification, and characterization described here in more detail are not only relevant to studies on other members of the glycoprotein hormone family, but also applicable to studies of other glycosylated proteins. Knowledge of structure-function relationships of specific hTSH domains is important for a better understanding of the molecular mechanisms of its action. New insights from such studies permit the design of glycoprotein hormone analogs with specific pharmacological properties and potential clinical applications.
Szkudlinski
M W
MW
Laboratory of Molecular Endocrinology, Department of Medicine, University of Maryland School of Medicine and the Institute of Human Virology, Medical Biotechnology Center, 725 West Lombard Street, Baltimore, Maryland 21201-1009, USA. szkudlin@umbi.umd.edu
Grossmann
M
M
Leitolf
H
H
Weintraub
B D
BD
D000818:Animals; D001681:Biological Assay / Q000379:methods; D002942:Circular Dichroism; D016208:Databases, Factual; D006801:Humans; D008297:Male; D008954:Models, Biological; D009154:Mutation; D009844:Oligosaccharides / Q000737:chemistry; D015202:Protein Engineering; D017434:Protein Structure, Tertiary; D051381:Rats; D011994:Recombinant Proteins / Q000138:chemical synthesis / Q000302:isolation & purification; D013329:Structure-Activity Relationship; D013972:Thyrotropin / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D013997:Time Factors
D009844:Oligosaccharides; D011994:Recombinant Proteins; D013972:Thyrotropin