HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bateman, A. Articles by Bennett, H. P. Search for Related Content PubMed PubMed Citation Articles by Bateman, A. Articles by Bennett, H. P. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 265, Issue 36, 22130-22136, 12, 1990

Post-translational modification of bovine pro-opiomelanocortin. Tyrosine sulfation and pyroglutamate formation, a mass spectrometric study

A Bateman, S Solomon and HP Bennett
Endocrine Laboratory, Royal Victoria Hospital, Montreal, Quebec, Canada.

The amino-terminal fragment of beta-lipotropin (i.e. beta-lipotropin (1- 40)) and joining peptide portions of pro-opiomelanocortin have been purified from extracts of bovine posterior pituitaries. Peptides were purified using a combination of reversed-phase and ion-exchange batch extraction procedures followed by reversed-phase high performance liquid chromatography. beta-Lipotropin (1-40) was found to consist of four major components while joining peptide was found to consist of two major components. Fast atom bombardment-mass spectrometric analysis of the tryptic fragments of both peptides revealed that the observed heterogeneity could be explained in terms of post-translational modifications. beta-Lipotropin (1-40) was found to be sulfated at tyrosine residue 28 to an extent of about 50%. The tyrosine residue in beta-lipotropin (1-40) is situated within an amino acid sequence with a preponderance of glutamate residues. Sulfation of this amino acid residue is entirely compatible with the known primary structure requirements of the sulfotransferase enzyme located in the trans-Golgi fraction. Both beta-lipotropin (1-40) and joining peptide were found to have pyroglutamate at their amino termini to an extent of about 50%. The cDNA sequence for bovine pro-opiomelanocortin predicts the presence of glutamic acid at position 1 of both peptides. Pyroglutamate is normally formed through the cyclization of glutamine. This reaction is thought to be catalyzed by a pyroglutamate forming enzyme located within the secretory granule fraction. Under certain circumstances peptides with glutamate at their amino termini may act as substrates for this enzyme.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				Y. Tomidokoro, T. Lashley, A. Rostagno, T. A. Neubert, M. Bojsen-Moller, H. Braendgaard, G. Plant, J. Holton, B. Frangione, T. Revesz, et al. Familial Danish Dementia: CO-EXISTENCE OF DANISH AND ALZHEIMER AMYLOID SUBUNITS (ADan AND A{beta}) IN THE ABSENCE OF COMPACT PLAQUES J. Biol. Chem., November 4, 2005; 280(44): 36883 - 36894. [Abstract] [Full Text] [PDF]

				J. A. Ghiso, J. Holton, L. Miravalle, M. Calero, T. Lashley, R. Vidal, H. Houlden, N. Wood, T. A. Neubert, A. Rostagno, et al. Systemic Amyloid Deposits in Familial British Dementia J. Biol. Chem., November 16, 2001; 276(47): 43909 - 43914. [Abstract] [Full Text] [PDF]

				Y. Furukawa, K. Nakamaru, H. Wakayama, Y. Fujisawa, H. Minakata, S. Ohta, F. Morishita, O. Matsushima, L. Li, E. Romanova, et al. The Enterins: A Novel Family of Neuropeptides Isolated from the Enteric Nervous System and CNS of Aplysia J. Neurosci., October 15, 2001; 21(20): 8247 - 8261. [Abstract] [Full Text] [PDF]

				A. Slominski, J. Wortsman, T. Luger, R. Paus, and S. Solomon Corticotropin Releasing Hormone and Proopiomelanocortin Involvement in the Cutaneous Response to Stress Physiol Rev, July 1, 2000; 80(3): 979 - 1020. [Abstract] [Full Text] [PDF]

				T. Sakurai, T. Moriguchi, K. Furuya, N. Kajiwara, T. Nakamura, M. Yanagisawa, and K. Goto Structure and Function of Human Prepro-orexin Gene J. Biol. Chem., June 18, 1999; 274(25): 17771 - 17776. [Abstract] [Full Text] [PDF]