JBC PeproTech; Our Business is Cytokines!

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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Frelinger, A. L.
Right arrow Articles by Zull, J. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Frelinger, A. L., 3d
Right arrow Articles by Zull, J. E.
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?

J. Biol. Chem., Vol. 259, Issue 9, 5507-5513, 05, 1984

Oxidized forms of parathyroid hormone with biological activity. Separation and characterization of hormone forms oxidized at methionine 8 and methionine 18

AL Frelinger 3d and JE Zull

Bovine parathyroid hormone (PTH) was oxidized with hydrogen peroxide, and the oxidation products were separated by reverse phase high performance liquid chromatography. Using a shallow gradient, four major peaks (peaks I-IV in order of elution) were identified and completely separated from one another. Peak IV co-eluted with fully reduced PTH. The earliest eluting peak (peak I) could be reduced with mercaptoethylamine to produce all three of the later eluting ones. The second peak could be reduced back to peak IV but not to peak III, while peak III could be oxidized to peak I but not to peak II. These data plus the kinetics of oxidation showed that peaks II and III are intermediate in the generation of I from IV or IV from I, but were not generated from one another. Amino acid analysis showed that peak I contains no methionine and two residues of methionine sulfoxide, peaks II and III one methionine sulfoxide each, and peak IV two residues of methionine and no sulfoxide. Study of the peptides produced from each form of PTH by cleavage with cyanogen bromide showed that peak II is oxidized at methionine 8 and peak III at methionine 18 while peak I is oxidized at both methionines. The biological activity of each peak was determined in the kidney membrane adenylyl cyclase assay. All forms were active but with widely varying potencies (peak IV greater than peak III greater than peak II greater than peak I).
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?


This article has been cited by other articles:


Home page
 ScienceHome page
M. Hunkapiller, J. Strickler, and K. Wilson
Contemporary methodology for protein structure determination
Science, October 19, 1984; 226(4672): 304 - 311.
[Abstract] [PDF]

Home page
 J. Biol. Chem.Home page
M. Shimizu, P. H. Carter, and T. J. Gardella
Autoactivation of Type-1 Parathyroid Hormone Receptors Containing a Tethered Ligand
J. Biol. Chem., June 23, 2000; 275(26): 19456 - 19460.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Shimizu, J. T. Potts Jr., and T. J. Gardella
Minimization of Parathyroid Hormone. NOVEL AMINO-TERMINAL PARATHYROID HORMONE FRAGMENTS WITH ENHANCED POTENCY IN ACTIVATING THE TYPE-1 PARATHYROID HORMONE RECEPTOR
J. Biol. Chem., July 14, 2000; 275(29): 21836 - 21843.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1984 by the American Society for Biochemistry and Molecular Biology.