JBC INTERFERin siRNA transfection reagent

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kohn, L. D.
Right arrow Articles by Winand, R. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kohn, L. D.
Right arrow Articles by Winand, R. J.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Relationship of Thyrotropin to Exophthalmos-producing Substance

FORMATION OF AN EXOPHTHALMOS-PRODUCING SUBSTANCE BY PEPSIN DIGESTION OF PITUITARY GLYCOPROTEINS CONTAINING BOTH THYROTROPIC AND EXOPHTHALMOGENIC ACTIVITY

Leonard D. Kohn 1 and Roger J. Winand 1

From the 1 From the Laboratory of Biochemical Pharmacology, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland 20014, and The Institute of Medicine, Department of Clinical Medicine and Semiology, University of Liège, Belgium

Homogeneous bovine pituitary glycoproteins with both thyrotropic and exophthalmogenic activity have been subjected to limited proteolysis by pepsin. One fraction lost 90% of its thyrotropin action, but only 15% of its exophthalmogenic activity, when incubated with a 1% weight ratio of pepsin at pH 2.2 and at 37°. Analytical disc gel analyses showed that the decrease in thyrotropin activity could be correlated with the destruction of the glycoprotein originally in this fraction and with the appearance of several new protein-staining bands. One of the digestion products was an oligosaccharide-containing derivative with terminal galactose on at least one of its carbohydrate moieties. After isolation by electrofocusing, this derivative was shown to have exophthalmogenic activity but to be without significant thyrotropin action; the residual thyrotropin activity of limited digests remained associated with nondigested glycoproteins containing both activities. The exophthalmogenic derivative had an isoelectric point at pH 6.9 and exhibited a single component on analytical disc gels. It had a molecular weight of 20,000 to 22,000 when evaluated by electrophoresis on gels containing sodium dodecyl sulfate, but appeared to be composed of two polypeptide units, one with a molecular weight of approximately 14,000 and the other with a molecular weight of approximately 6,000. The results indicate that limited proteolysis of a homogeneous pituitary glycoprotein with both thyrotropic and exophthalmogenic activity can yield a derivative uniquely active as an exophthalmos-producing substance.

Submitted on July 7, 1971


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?





HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1971 by the American Society for Biochemistry and Molecular Biology.