Oxygen binding of erythrocruorin and coelomic cell haemoglobin from the terebellid polychaete Neoamphitrite figulus related to some environmental factors

1982 ◽  
Vol 62 (2) ◽  
pp. 373-384 ◽  
Author(s):  
Rufus M. G. Wells ◽  
Lynda M. Warren
Keyword(s):  
Haemoglobin Concentration ◽  
Log P ◽  
Oxygen Binding ◽  
Transfer System ◽  
Equilibrium Curve ◽  
High Affinity ◽  
Coelomic Cells ◽  
Hyperbolic Equilibrium ◽  
Oxygen Equilibrium Curve

Measurements of pH, oxygen content, O2-combining capacity, and haemoglobin concentration were made for the vascular blood of the burrowing polychaete Neoamphitrite figulus in order to assess the role of its two respiratory pigments in respiration. The oxygen equilibrium curve of the erythrocruorin (extracellular haemoglobin) in the vessels was sigmoidal, having an n50 value of 1·5 and a low affinity for oxygen as determined by the P50 which was 26 mmHg at pH 7·31 and 18 °C. O2-binding by the erythrocruorin is sensitive to changes in pH (Δ log P50/Δ log pH = –0·24 to –0·29). The coelomic cell haemoglobin has a hyperbolic equilibrium curve (n50 = 1·0) and a high affinity for oxygen (P50 = 4·5 mmHg) independent of pH, suggesting an oxygen transfer system from the erythrocruorin to the coelomic cells.

scholarly journals The interplay of temperature and protons in the modulation of oxygen binding by squid blood

1992 ◽  
Vol 281 (3) ◽  
pp. 725-728 ◽  
Author(s):  
B Giardina ◽  
S G Condò ◽  
O Brix
Keyword(s):  
Rangifer Tarandus ◽  
Effect Of Temperature ◽  
Strong Temperature Dependence ◽  
Oxygen Binding ◽  
Experimental Conditions ◽  
Ovibos Moschatus ◽  
High Affinity ◽  
Loading And Unloading ◽  
Musk Ox ◽  
Oxygen Equilibrium Curve

An extensive set of data relating to the binding of oxygen by haemocyanin from the squid Todarodes sagittatus has been collected under various experimental conditions. The results obtained show that, within the range of physiological pH, the concentration of protons affects mainly the high-affinity state of the molecule without significantly affecting the low-affinity state. As far as the effect of temperature is concerned, the data show a characteristic feature which is very similar to that previously described in the case of haemoglobins from Arctic mammals such as reindeer (Rangifer tarandus) and musk ox. (Ovibos moschatus). The shape of the oxygen equilibrium curve shows strong temperature-dependence, since the overall heat of the binding of oxygen to the low-affinity state of the molecule is strongly exothermic and that to the high-affinity state is very close to zero. The results provide an outline of the intramolecular compromise that, through the interplay of temperature and protons, optimizes the loading and unloading of oxygen under the various environmental conditions experienced by this species of squid.

Effect of haemoglobin concentration on the oxygen affinity of intact lamprey erythrocytes

1995 ◽  
Vol 198 (11) ◽  
pp. 2393-2396 ◽  
Author(s):  
S Airaksinen ◽  
M Nikinmaa
Keyword(s):  
Blood Cell ◽  
Red Blood Cell ◽  
Haemoglobin Concentration ◽  
Oxygen Affinity ◽  
Equilibrium Curve ◽  
Volume Changes ◽  
Oxygen Equilibrium ◽  
The Mean ◽  
The Right ◽  
Oxygen Equilibrium Curve

We investigated whether the oxygen affinity of lamprey haemoglobin decreases with increasing oxygen concentration at the high (10­25 mmol l-1 monomeric) haemoglobin concentrations prevailing within the erythrocytes. The intracellular concentration of haemoglobin was experimentally adjusted by shrinking the cells osmotically: the osmolality of the equilibration medium was increased from approximately 250 mosmol kg-1 by 90 mosmol kg-1 to 340 mosmol kg-1 or by 180 mosmol kg-1 to 430 mosmol kg-1 by adding sucrose in the medium. This increased the mean cellular haemoglobin concentration from 16.9±0.23 mmol l-1 (monomeric haemoglobin) to 20.0±0.20 mmol l-1 (monomeric haemoglobin) and to 23.0±0.36 mmol l-1 (monomeric haemoglobin), respectively (means ± s.e.m., N=35­40; all the samples from 7­8 different pools of blood at each osmolality combined). The oxygen equilibrium curves at each osmolality were determined by Tucker's method. An increase in haemoglobin concentration shifted the oxygen equilibrium curve to the right as indicated by the P50 values, which were 4.26±0.07 kPa at the lowest, 4.64±0.13 kPa at the intermediate and 5.64±0.40 kPa (means ± s.e.m., N=7­8) at the highest haemoglobin concentrations. The decrease in haemoglobin oxygen-affinity was attributed to the volume changes, since the intracellular pH did not decrease with increasing mean cellular haemoglobin concentration. Thus, the variations in red blood cell volume commonly observed during hypoxia may play a role in the regulation of haemoglobin function.

Molecular adaptation of the blood of Antarctic teleosts to environmental conditions

1989 ◽  
Vol 1 (2) ◽  
pp. 119-124 ◽  
Author(s):  
Guido Di Prisco ◽  
Rossana D'Avino
Keyword(s):  
Haemoglobin Concentration ◽  
Oxygen Binding ◽  
Root Effect ◽  
Physiological Relevance ◽  
Antarctic Convergence ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
The Antarctic ◽  
The Relationship ◽  
Antarctic Teleosts

Following the break-up of Gondwana, the drift of Antarctica to its present position and the establishment of the Antarctic Convergence, fish evolution was characterized by adaptation to progressive cooling of the environment. The decrease of erythrocyte number and haemoglobin concentration in the blood of Antarctic teleosts raises several questions concerning the physiology of respiration and the enzymatic role of erythrocytes. Our study of the molecular basis of cold adaptation includes the relationship between molecular structure and biological function of haemoglobins. Species of the suborder Notothenioidei, largely confined within the Convergence, have only one major haemoglobin, which displays the Root effect in oxygen binding; on the other hand, Zoarcidae (a family found at all latitudes) have four or five haemoglobins, only one of which displays the Root effect. In addition, our data indicate that the physiological relevance of erythrocyte-like cells, present in very small number in the blood of haemoglobinless Channichthyidae, may be linked to higher content of enzymes, such as glucose-6-phosphate dehydrogenase, in comparison with erythrocytes of red-blooded fishes.

Blood oxygen transport in the free-swimming hagfish, Eptatretus cirrhatus

1986 ◽  
Vol 123 (1) ◽  
pp. 43-53 ◽  
Author(s):  
R. M. Wells ◽  
M. E. Forster ◽  
W. Davison ◽  
H. H. Taylor ◽  
P. S. Davie ◽  
...  
Keyword(s):  
Venous Blood ◽  
Mixed Venous Blood ◽  
Oxygen Binding ◽  
Blood Oxygen ◽  
Binding Data ◽  
Gas Measurements ◽  
Hyperbolic Equilibrium

Arterial and mixed venous blood were sampled through chronically implanted cannulae from rested and swimming hagfish. PaO2 remained high when hagfish were swum for 15 min at a velocity of 20 cm s-1. PvO2 fell from 17.2 mmHg at rest to 3.5 mmHg after swimming, and the arteriovenous pH difference increased from 0.15 to 0.25 pH units. Whole blood oxygen equilibrium curves were essentially hyperbolic (Hill's n value = 1.38) and gave a half-saturation PO2 (P50) value of 12.3 mmHg at pH 7.8 and 16 degrees C. A CO2-Bohr factor (phi = delta logP50/delta pH) of −0.43 and a limited buffering capacity of the blood, amounting to approx. 4 slykes, were observed. The role of the blood in transporting oxygen and carbon dioxide both at rest and after swimming is established by in vivo blood gas measurements and in vitro oxygen-binding data. The low internal PvO2 at rest is close to the P50 measured under similar conditions and the hyperbolic equilibrium curve permits further oxygen unloading when PvO2 falls during swimming.

The Role of the Initiator System in the Synthesis of Acidic Multifunctional Nanoparticles Designed for Molecular Imprinting of Proteins

2020 ◽  
Vol 65 (1) ◽  
pp. 28-41
Author(s):  
Marwa Aly Ahmed ◽  
Júlia Erdőssy ◽  
Viola Horváth
Keyword(s):  
Acrylic Acid ◽  
Binding Affinity ◽  
Molecular Imprinting ◽  
Low Temperatures ◽  
Ammonium Persulfate ◽  
Sodium Bisulfite ◽  
Multifunctional Nanoparticles ◽  
High Affinity ◽  
Initiator System

Multifunctional nanoparticles have been shown earlier to bind certain proteins with high affinity and the binding affinity could be enhanced by molecular imprinting of the target protein. In this work different initiator systems were used and compared during the synthesis of poly (N-isopropylacrylamide-co-acrylic acid-co-N-tert-butylacrylamide) nanoparticles with respect to their future applicability in molecular imprinting of lysozyme. The decomposition of ammonium persulfate initiator was initiated either thermally at 60 °C or by using redox activators, namely tetramethylethylenediamine or sodium bisulfite at low temperatures. Morphology differences in the resulting nanoparticles have been revealed using scanning electron microscopy and dynamic light scattering. During polymerization the conversion of each monomer was followed in time. Striking differences were demonstrated in the incorporation rate of acrylic acid between the tetramethylethylenediamine catalyzed initiation and the other systems. This led to a completely different nanoparticle microstructure the consequence of which was the distinctly lower lysozyme binding affinity. On the contrary, the use of sodium bisulfite activation resulted in similar nanoparticle structural homogeneity and protein binding affinity as the thermal initiation.

Acid-Sensing Ion Channels

2020 ◽  
Author(s):  
Stefan Gründer
Keyword(s):  
Nervous System ◽  
Ion Channels ◽  
Excitatory Synapses ◽  
Detailed Characterization ◽  
High Affinity ◽  
Acid Sensing Ion Channels ◽  
Long Time ◽  
Pathological Pain

Acid-sensing ion channels (ASICs) are proton-gated Na+ channels. Being almost ubiquitously present in neurons of the vertebrate nervous system, their precise function remained obscure for a long time. Various animal toxins that bind to ASICs with high affinity and specificity have been tremendously helpful in uncovering the role of ASICs. We now know that they contribute to synaptic transmission at excitatory synapses as well as to sensing metabolic acidosis and nociception. Moreover, detailed characterization of mouse models uncovered an unanticipated role of ASICs in disorders of the nervous system like stroke, multiple sclerosis, and pathological pain. This review provides an overview on the expression, structure, and pharmacology of ASICs plus a summary of what is known and what is still unknown about their physiological functions and their roles in diseases.

scholarly journals Oxygen equilibrium curve of normal human blood and its evaluation by Adair's equation.

1977 ◽  
Vol 252 (7) ◽  
pp. 2331-2337 ◽  
Author(s):  
R M Winslow ◽  
M L Swenberg ◽  
R L Berger ◽  
R I Shrager ◽  
M Luzzana ◽  
...  
Keyword(s):  
Human Blood ◽  
Equilibrium Curve ◽  
Oxygen Equilibrium ◽  
Normal Human ◽  
Oxygen Equilibrium Curve ◽  
Normal Human Blood

scholarly journals Novel Three-Finger Neurotoxins from Naja melanoleuca Cobra Venom Interact with GABAA and Nicotinic Acetylcholine Receptors

Toxins ◽  
2021 ◽  
Vol 13 (2) ◽  
pp. 164
Author(s):  
Lina Son ◽  
Elena Kryukova ◽  
Rustam Ziganshin ◽  
Tatyana Andreeva ◽  
Denis Kudryavtsev ◽  
...  
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Gabaa Receptors ◽  
Binding Sites ◽  
Acetylcholine Receptors ◽  
Nicotinic Acetylcholine ◽  
High Affinity ◽  
Central Loop ◽  
Acetylcholine Binding Proteins ◽  
Α7 Nachrs

Cobra venoms contain three-finger toxins (TFT) including α-neurotoxins efficiently binding nicotinic acetylcholine receptors (nAChRs). As shown recently, several TFTs block GABAA receptors (GABAARs) with different efficacy, an important role of the TFTs central loop in binding to these receptors being demonstrated. We supposed that the positive charge (Arg36) in this loop of α-cobratoxin may explain its high affinity to GABAAR and here studied α-neurotoxins from African cobra N. melanoleuca venom for their ability to interact with GABAARs and nAChRs. Three α-neurotoxins, close homologues of the known N. melanoleuca long neurotoxins 1 and 2, were isolated and sequenced. Their analysis on Torpedocalifornica and α7 nAChRs, as well as on acetylcholine binding proteins and on several subtypes of GABAARs, showed that all toxins interacted with the GABAAR much weaker than with the nAChR: one neurotoxin was almost as active as α-cobratoxin, while others manifested lower activity. The earlier hypothesis about the essential role of Arg36 as the determinant of high affinity to GABAAR was not confirmed, but the results obtained suggest that the toxin loop III may contribute to the efficient interaction of some long-chain neurotoxins with GABAAR. One of isolated toxins manifested different affinity to two binding sites on Torpedo nAChR.

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