Studies on Yak Hemoglobin(Bos grunniens,Bovidae): Structural Basis for High Intrinsic Oxygen Affinity?

1985 ◽  
Vol 366 (1) ◽  
pp. 63-68 ◽  
Author(s):  
Ralte LALTHANTLUANGA ◽  
Henning WIESNER ◽  
Gerhard BRAUNITZER
Keyword(s):  
Oxygen Affinity ◽  
Structural Basis ◽  
Bos Grunniens

Structures of haemoglobin from woolly mammoth in liganded and unliganded states

2012 ◽  
Vol 68 (11) ◽  
pp. 1441-1449 ◽  
Author(s):  
Hiroki Noguchi ◽  
Kevin L. Campbell ◽  
Chien Ho ◽  
Satoru Unzai ◽  
Sam-Yong Park ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Crystal Structures ◽  
High Latitude ◽  
Quaternary Structure ◽  
Globin Gene ◽  
Oxygen Affinity ◽  
Chloride Ions ◽  
Structural Basis ◽  
Structure Changes ◽  
Woolly Mammoth

The haemoglobin (Hb) of the extinct woolly mammoth has been recreated using recombinant genes expressed inEscherichia coli. The globin gene sequences were previously determined using DNA recovered from frozen cadavers. Although highly similar to the Hb of existing elephants, the woolly mammoth protein shows rather different responses to chloride ions and temperature. In particular, the heat of oxygenation is found to be much lower in mammoth Hb, which appears to be an adaptation to the harsh high-latitude climates of the Pleistocene Ice Ages and has been linked to heightened sensitivity of the mammoth protein to protons, chloride ions and organic phosphates relative to that of Asian elephants. To elucidate the structural basis for the altered homotropic and heterotropic effects, the crystal structures of mammoth Hb have been determined in the deoxy, carbonmonoxy and aquo-met forms. These models, which are the first structures of Hb from an extinct species, show many features reminiscent of human Hb, but underline how the delicate control of oxygen affinity relies on much more than simple overall quaternary-structure changes.

scholarly journals Tertiary and quaternary structural basis of oxygen affinity in human hemoglobin as revealed by multiscale simulations

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Mauro Bringas ◽  
Ariel A. Petruk ◽  
Darío A. Estrin ◽  
Luciana Capece ◽  
Marcelo A. Martí
Keyword(s):  
Oxygen Affinity ◽  
Structural Basis ◽  
Multiscale Simulations ◽  
Human Hemoglobin

Structures of R- and T-state hemoglobin Bassett: elucidating the structural basis for the low oxygen affinity of a mutant hemoglobin

2005 ◽  
Vol 61 (2) ◽  
pp. 156-162 ◽  
Author(s):  
Martin K. Safo ◽  
Osheiza Abdulmalik ◽  
Hsiang-Ru Lin ◽  
Toshio Asakura ◽  
Donald J. Abraham
Keyword(s):  
Oxygen Affinity ◽  
Structural Basis ◽  
Low Oxygen ◽  
T State ◽  
Low Oxygen Affinity

Effects of temperature acclimation on crayfish hemocyanin oxygen binding

1981 ◽  
Vol 240 (1) ◽  
pp. R93-R98 ◽  
Author(s):  
P. S. Rutledge
Keyword(s):  
Narrow Range ◽  
Oxygen Affinity ◽  
Temperature Acclimation ◽  
Structural Basis ◽  
Acclimation Temperature ◽  
Oxygen Binding ◽  
Functional Changes ◽  
Acclimation Response ◽  
Effects Of Temperature ◽  
Range Of Values

Crayfish, Pacifastacus leniusculus, were acclimated to 10, 20, and 25 degrees C for 1 mo. Hemocyanin from animals at these three acclimation temperatures showed distinctly different oxygen binding patterns. At any particular set of test temperature and pH, hemocyanin from 10 degrees C-acclimated animals had the lowest oxygen affinity and the greatest cooperativity, whereas hemocyanin from 25 degrees C-acclimated animals had the highest oxygen affinity and the lowest cooperativity. When tested at their own acclimation temperature, and at normal hemolymph pH for that temperature, all three hemocyanins showed oxygen pressure for half-saturation of hemoglobin of 6-7 Torr. Thus acclimation keeps oxygen affinity centered around a narrow range of values. The acclimation response probably eliminates hemocyanin oxygen affinity as a major factor in the decline of oxygen uptake ability in the crayfish above 20 degrees C. The structural basis for the observed functional changes in the hemocyanin is not yet clear.

An Additional H-Bond in the α1β2Interface as the Structural Basis for the Low Oxygen Affinity and High Cooperativity of a Novel Recombinant Hemoglobin (βL105W)†

Biochemistry ◽  
2000 ◽  
Vol 39 (45) ◽  
pp. 13708-13718 ◽  
Author(s):  
Tsuei-Yun Fang ◽  
Virgil Simplaceanu ◽  
Ching-Hsuan Tsai ◽  
Nancy T. Ho ◽  
Chien Ho
Keyword(s):  
Oxygen Affinity ◽  
Structural Basis ◽  
Low Oxygen ◽  
Low Oxygen Affinity

scholarly journals Deer mouse hemoglobin exhibits a lowered oxygen affinity owing to mobility of the E helix

2013 ◽  
Vol 69 (4) ◽  
pp. 393-398 ◽  
Author(s):  
Noriko Inoguchi ◽  
Jake R. Oshlo ◽  
Chandrasekhar Natarajan ◽  
Roy E. Weber ◽  
Angela Fago ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Deer Mouse ◽  
Oxygen Affinity ◽  
Exchange Chromatography ◽  
Structural Basis ◽  
Diffusion Method ◽  
Hanging Drop ◽  
Functional Variation ◽  
Orthorhombic Crystal ◽  
Hemoglobin Oxygen Affinity

The deer mouse,Peromyscus maniculatus, exhibits altitude-associated variation in hemoglobin oxygen affinity. To examine the structural basis of this functional variation, the structure of the hemoglobin was solved. Recombinant hemoglobin was expressed inEscherichia coliand was purified by ion-exchange chromatography. Recombinant hemoglobin was crystallized by the hanging-drop vapor-diffusion method using polyethylene glycol as a precipitant. The obtained orthorhombic crystal contained two subunits in the asymmetric unit. The refined structure was interpreted as the aquo-met form. Structural comparisons were performed among hemoglobins from deer mouse, house mouse and human. In contrast to human hemoglobin, deer mouse hemoglobin lacks the hydrogen bond between α1Trp14 in the A helix and α1Thr67 in the E helix owing to the Thr67Ala substitution. In addition, deer mouse hemoglobin has a unique hydrogen bond at the α1β1 interface between residues α1Cys34 and β1Ser128.

Novel Water-Mediated Hydrogen Bonds as the Structural Basis for the Low Oxygen Affinity of the Blood Substitute Candidate rHb(α96Val→Trp)†,‡

Biochemistry ◽  
1998 ◽  
Vol 37 (26) ◽  
pp. 9258-9265 ◽  
Author(s):  
Yoram A. Puius ◽  
Ming Zou ◽  
Nancy T. Ho ◽  
Chien Ho ◽  
Steven C. Almo
Keyword(s):  
Hydrogen Bonds ◽  
Oxygen Affinity ◽  
Blood Substitute ◽  
Structural Basis ◽  
Low Oxygen ◽  
Low Oxygen Affinity

Organization of tight junctions in the choroid plexus epithelium

1978 ◽  
Vol 36 (2) ◽  
pp. 336-337
Author(s):  
B. Van Deurs ◽  
J. K. Koehler
Keyword(s):  
Choroid Plexus ◽  
Present Report ◽  
Freeze Fracture ◽  
Barrier Properties ◽  
Cell Junctions ◽  
Structural Basis ◽  
Apical Surface ◽  
Choroid Plexus Epithelium ◽  
Solid Nitrogen ◽  
Special Composition

The choroid plexus epithelium constitutes a blood-cerebrospinal fluid (CSF) barrier, and is involved in regulation of the special composition of the CSF. The epithelium is provided with an ouabain-sensitive Na/K-pump located at the apical surface, actively pumping ions into the CSF. The choroid plexus epithelium has been described as “leaky” with a low transepithelial resistance, and a passive transepithelial flux following a paracellular route (intercellular spaces and cell junctions) also takes place. The present report describes the structural basis for these “barrier” properties of the choroid plexus epithelium as revealed by freeze fracture.Choroid plexus from the lateral, third and fourth ventricles of rats were used. The tissue was fixed in glutaraldehyde and stored in 30% glycerol. Freezing was performed either in liquid nitrogen-cooled Freon 22, or directly in a mixture of liquid and solid nitrogen prepared in a special vacuum chamber. The latter method was always used, and considered necessary, when preparations of complementary (double) replicas were made.

High resolution spot scan imaging of frozen, hydrated actin bundles with 400kV electrons

1992 ◽  
Vol 50 (1) ◽  
pp. 512-513
Author(s):  
J. Jakana ◽  
M.F. Schmid ◽  
P. Matsudaira ◽  
W. Chiu
Keyword(s):  
High Resolution ◽  
Binding Proteins ◽  
Actin Binding ◽  
Eukaryotic Cells ◽  
Dimensional Structure ◽  
Structural Basis ◽  
Actin Bundle ◽  
Actin Bundles ◽  
3 Dimensional ◽  
Macromolecular Assembly

Actin is a protein found in all eukaryotic cells. In its polymerized form, the cells use it for motility, cytokinesis and for cytoskeletal support. An example of this latter class is the actin bundle in the acrosomal process from the Limulus sperm. The different functions actin performs seem to arise from its interaction with the actin binding proteins. A 3-dimensional structure of this macromolecular assembly is essential to provide a structural basis for understanding this interaction in relationship to its development and functions.

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