help button home button Endocrine Society JCEM JCEM Call for Nominations for EIC
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text (PDF)
Right arrow Submit a related Letter to the Editor
Right arrow Purchase Article
Right arrow View Shopping Cart
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kratzsch, J.
Right arrow Articles by Birkenmeier, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kratzsch, J.
Right arrow Articles by Birkenmeier, G.

Journal of Clinical Endocrinology & Metabolism, Vol 80, 585-590, Copyright © 1995 by Endocrine Society

ARTICLES

Identification of transformed alpha 2-macroglobulin as a growth hormone- binding protein in human blood

J Kratzsch, T Selisko and G Birkenmeier
Institute of Clinical Chemistry, University of Leipzig, Germany.

We have found that the human GH forms complexes with the purified proteinase inhibitor, alpha 2-macroglobulin. This inhibitor occurs in two different forms in human blood, known as native and transformed alpha 2-macroglobulin. It could be clearly demonstrated by chromatography and electrophoresis combined with autoradiography that the GH binds specifically to the transformed inhibitor, but not to the native protein. The binding was characterized as being mainly noncovalent to specific binding sites present only in the transformed inhibitor molecule. Binding analysis using antibody precipitation technique revealed two different classes of binding sites with dissociation constants of 0.49 +/- 0.12 and 61 +/- 8 mumol/L for high and low affinity binding sites, respectively. Distribution analysis of 125I-labeled GH in whole plasma suggested that the hormone is bound to different proteins: 1) to the high affinity GH-binding protein, and 2) to the low affinity GH-binding protein identified as transformed alpha 2-macroglobulin.


This article has been cited by other articles:


Home page
 J. Clin. Endocrinol. Metab.Home page
A. Korner, A. Garten, M. Bluher, R. Tauscher, J. Kratzsch, and W. Kiess
Molecular Characteristics of Serum Visfatin and Differential Detection by Immunoassays
J. Clin. Endocrinol. Metab., December 1, 2007; 92(12): 4783 - 4791.
[Abstract] [Full Text] [PDF]

Home page
 IOVSHome page
E. J. Sanders, M. A. Walter, E. Parker, C. Aramburo, and S. Harvey
Opticin Binds Retinal Growth Hormone in the Embryonic Vitreous
Invest. Ophthalmol. Vis. Sci., December 1, 2003; 44(12): 5404 - 5409.
[Abstract] [Full Text] [PDF]

Home page
 EndocrinologyHome page
K.-C. Leung, N. Doyle, and K. K. Y. Ho
Characterization of a Low Affinity Binding Protein for Growth Hormone in Rat Serum
Endocrinology, January 1, 2000; 141(1): 138 - 145.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Patel, E. C. M. B.-V. d. Linden, S. W. Altmann, K. Gish, S. Balasubramanian, J. C. Timans, D. Peterson, M. P. Bell, J. F. Bazan, A. Varki, et al.
OB-BP1/Siglec-6. A LEPTIN- AND SIALIC ACID-BINDING PROTEIN OF THE IMMUNOGLOBULIN SUPERFAMILY
J. Biol. Chem., August 6, 1999; 274(32): 22729 - 22738.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Endocrinology Endocrine Reviews J. Clin. End. & Metab.
Molecular Endocrinology Recent Prog. Horm. Res. All Endocrine Journals
Copyright © 1995 by The Endocrine Society