|
|
|
|||||||
|
|||||||||
J Biol Chem, Vol. 273, Issue 27, 16998-17011, July 3, 1998
From the Hemoglobin (Hb) occurs in circulating red blood
cells, neural tissue, and body wall muscle tissue of the nemertean
worm, Cerebratulus lacteus. The neural and body wall tissue
each express single major Hb components for which the amino acid
sequences have been deduced from cDNA and genomic DNA. These
109-residue globins form the smallest stable Hbs known. The globin
genes have three exons and two introns with splice sites in the highly
conserved positions of most globin genes. Alignment of the sequences
with those of other globins indicates that the A, B, and H helices are
about one-half the typical length. Phylogenetic analysis indicates that shortening results in a small tendency of globins to group together regardless of their actual relationships. The neural and body wall Hbs
in situ are half-saturated with O2 at 2.9 and
4.1 torr, respectively. The Hill coefficient for the neural Hb in
situ, ~2.9, suggests that the neural Hb self-associates in the
deoxy state at least to tetramers at the 2-3 mM (heme)
concentration estimated in the cells. The Hb must dissociate upon
oxygenation and dilution because the weight-average molecular mass of
the HbO2 in vitro is only about 18 kDa at 2-3
µM heme concentration. Calculations suggest that the Hb
can function as an O2 store capable of extending neuronal
activity in an anoxic environment for 5-30 min.
The Mini-hemoglobins in Neural and Body Wall Tissue of the
Nemertean Worm, Cerebratulus lacteus
,,,
, and
Department of Zoology, University of Texas,
Austin, Texas 78712-1064 and the Department of Biological
Sciences, Clemson University, Clemson, South Carolina 29631
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  M. D. Salter, K. Nienhaus, G. U. Nienhaus, S. Dewilde, L. Moens, A. Pesce, M. Nardini, M. Bolognesi, and J. S. Olson The Apolar Channel in Cerebratulus lacteus Hemoglobin Is the Route for O2 Entry and Exit J. Biol. Chem., December 19, 2008; 283(51): 35689 - 35702. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Ostojic, D. S. Sakaguchi, Y. de Lathouder, M. S. Hargrove, J. T. Trent III, Y. H. Kwon, R. H. Kardon, M. H. Kuehn, D. M. Betts, and S. Grozdanic Neuroglobin and cytoglobin: oxygen-binding proteins in retinal neurons. Invest. Ophthalmol. Vis. Sci., March 1, 2006; 47(3): 1016 - 1023. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Pesce, M. Nardini, P. Ascenzi, E. Geuens, S. Dewilde, L. Moens, M. Bolognesi, A. F. Riggs, A. Hale, P. Deng, et al. Thr-E11 Regulates O2 Affinity in Cerebratulus lacteus Mini-hemoglobin J. Biol. Chem., August 6, 2004; 279(32): 33662 - 33672. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Uno, D. Ryu, H. Tsutsumi, Y. Tomisugi, Y. Ishikawa, A. J. Wilkinson, H. Sato, and T. Hayashi Residues in the Distal Heme Pocket of Neuroglobin: IMPLICATIONS FOR THE MULTIPLE LIGAND BINDING STEPS J. Biol. Chem., February 13, 2004; 279(7): 5886 - 5893. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Dewilde, L. Kiger, T. Burmester, T. Hankeln, V. Baudin-Creuza, T. Aerts, M. C. Marden, R. Caubergs, and L. Moens Biochemical Characterization and Ligand Binding Properties of Neuroglobin, a Novel Member of the Globin Family J. Biol. Chem., October 12, 2001; 276(42): 38949 - 38955. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. E. Weber and S. N. Vinogradov Nonvertebrate Hemoglobins: Functions and Molecular Adaptations Physiol Rev, April 1, 2001; 81(2): 569 - 628. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. Qiu, D. H. Maillett, J. Knapp, J. S. Olson, and A. F. Riggs Lamprey Hemoglobin. STRUCTURAL BASIS OF THE BOHR EFFECT J. Biol. Chem., April 28, 2000; 275(18): 13517 - 13528. [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 |