spacer gif spacer gif spacer gif spacer gif Online submission spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow References
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 Jensen, F. B.
Right arrow Articles by Weber, R. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jensen, F. B.
Right arrow Articles by Weber, R. E.

Journal of Experimental Biology, Vol 201, Issue 19 2685-2690, Copyright © 1998 by Company of Biologists

JOURNAL ARTICLES

Interaction between haemoglobin and synthetic peptides of the N-terminal cytoplasmic fragment of trout band 3 (AE1) protein

FB Jensen, MH Jakobsen and RE Weber
Institute of Biology, Odense University, DK-5230 Odense M, Denmark. fbj@biology.ou.dk

Two acidic peptides corresponding to the first 10 and 20 amino acid residues of the N-terminal, cytoplasmic fragment of rainbow trout band 3 (AE1) protein were synthesised in order to study their interaction with trout and human haemoglobin (Hb). The peptides did not influence the oxygen affinity of the main anodic trout Hb component (Hb IV) when tested at surplus peptide concentration ([peptide]/[Hb4]=16), at high and low ionic strength and at pH values ranging from 6.5 to 7.6. With human Hb, however, the 20-mer peptide markedly decreased the oxygen affinity and increased the Bohr effect. These data suggest that the trout band 3 peptide binds preferentially to the deoxy (T) conformation of human Hb, probably at the organic phosphate binding site in the central cavity between the beta-chains, which is known to be the binding site for the acidic N terminus of human band 3. In trout Hb IV, the presence of negatively charged Asp at position NA2 of the beta-chains (in contrast to positive or neutral residues in mammalian Hb) may weaken any interaction with the highly negatively charged peptides.


This article has been cited by other articles:


Home page
 Am. J. Physiol. Regul. Integr. Comp. Physiol.Home page
R. E. Weber, W. Voelter, A. Fago, H. Echner, E. Campanella, and P. S. Low
Modulation of red cell glycolysis: interactions between vertebrate hemoglobins and cytoplasmic domains of band 3 red cell membrane proteins
Am J Physiol Regulatory Integrative Comp Physiol, August 1, 2004; 287(2): R454 - R464.
[Abstract] [Full Text] [PDF]

Home page
 J. Exp. Biol.Home page
R. E. Weber, S. Hourdez, F. Knowles, and F. Lallier
Hemoglobin function in deep-sea and hydrothermal-vent endemic fish: Symenchelis parasitica (Anguillidae) and Thermarces cerberus (Zoarcidae)
J. Exp. Biol., August 1, 2003; 206(15): 2693 - 2702.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. E. Weber, A. Fago, A. L. Val, A. Bang, M.-L. Van Hauwaert, S. Dewilde, F. Zal, and L. Moens
Isohemoglobin Differentiation in the Bimodal-breathing Amazon Catfish Hoplosternum littorale
J. Biol. Chem., June 2, 2000; 275(23): 17297 - 17305.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 1998