Oxygen Binding by the Metalloproteins Hemerythrin, Hemocyanin, and Hemoglobin

Author(s):  
Thomas M. Loehr
Keyword(s):  
Author(s):  
T. Wichertjes ◽  
E.J. Kwak ◽  
E.F.J. Van Bruggen

Hemocyanin of the horseshoe crab (Limulus polyphemus) has been studied in nany ways. Recently the structure, dissociation and reassembly was studied using electron microscopy of negatively stained specimens as the method of investigation. Crystallization of the protein proved to be possible and X-ray crystallographic analysis was started. Also fluorescence properties of the hemocyanin after dialysis against Tris-glycine buffer + 0.01 M EDTA pH 8.9 (so called “stripped” hemocyanin) and its fractions II and V were studied, as well as functional properties of the fractions by NMR. Finally the temperature-jump method was used for assaying the oxygen binding of the dissociating molecule and of preparations of isolated subunits. Nevertheless very little is known about the structure of the intact molecule. Schutter et al. suggested that the molecule possibly consists of two halves, combined in a staggered way, the halves themselves consisting of four subunits arranged in a square.


Author(s):  
E.R. Henry ◽  
J. Harper ◽  
K. Glass ◽  
B. Metaferia ◽  
J.M. Louis ◽  
...  

1994 ◽  
Vol 269 (39) ◽  
pp. 24114-24119
Author(s):  
M.T. Wilson ◽  
G. Antonini ◽  
F. Malatesta ◽  
P. Sarti ◽  
M. Brunori

Biochemistry ◽  
2005 ◽  
Vol 44 (36) ◽  
pp. 11925-11938 ◽  
Author(s):  
Jo M. Holt ◽  
Alexandra L. Klinger ◽  
Connie S. Yarian ◽  
Varsha Keelara ◽  
Gary K. Ackers

2005 ◽  
Vol 169 (2) ◽  
pp. 251-256 ◽  
Author(s):  
C. Cambier ◽  
N. Di Passio ◽  
T. Clerbaux ◽  
H. Amory ◽  
V. Marville ◽  
...  
Keyword(s):  

Author(s):  
Maria T. Sanna ◽  
Alessandra Olianas ◽  
Massimo Castagnola ◽  
Luigi Sollai ◽  
Barbara Manconi ◽  
...  
Keyword(s):  

1976 ◽  
Vol 51 (2) ◽  
pp. 185-188
Author(s):  
P. M. Tweeddale ◽  
R. J. E. Leggett ◽  
D. C. Flenley

1. Oxygen-binding, plasma and intra-erythrocytic pH, and haemoglobin, 2,3-diphosphoglycerate and inorganic phosphate concentrations were measured in sixty-two healthy non-smokers aged between 18 and 89 years. 2. P50 (oxygen tension at 50% oxygen saturation) expressed at plasma pH 7·40 and Pco2 5·33 kPa showed a positive correlation with age. 3. This correlation of P50 with age was closer when P50 was expressed at a constant intra-erythrocytic pH 7·20. On average P50 at intra-erythrocytic pH 7·20 increased from 3·59 kPa at 20 years to 3·96 kPa at 90 years of age. 4. 2,3-Diphosphoglycerate, inorganic phosphate, haemoglobin and mean corpuscular haemoglobin concentrations did not correlate with P50 or with age.


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