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Topic:Hemoglobin

Hemoglobin is an iron-containing protein found in the red blood cells of horses, responsible for the transport of oxygen from the lungs to the tissues and the return of carbon dioxide from the tissues to the lungs. It plays a vital role in maintaining cellular respiration and energy metabolism. The structure and function of hemoglobin can be influenced by various factors, including genetics, age, and health status. Research into equine hemoglobin includes studies on its biochemical properties, the impact of different physiological and pathological conditions on its levels, and its importance in performance and endurance. This page compiles peer-reviewed research studies and scholarly articles that explore the characteristics, regulation, and clinical implications of hemoglobin in equine physiology and health.
PCV, Hb and plasma electrolyte studies in horses. II. The effects of surgical operations under chloroform anaesthesia on PCV, Hb and plasma electrolyte concentrations in horses.
The British veterinary journal    January 1, 1969   Volume 125, Issue 1 1-11 doi: 10.1016/s0007-1935(17)49157-3
Littlejohn A.No abstract available
PCV, Hb and plasma electrolyte studies in horses. I. Mean values in clinically normal horses.
The British veterinary journal    December 1, 1968   Volume 124, Issue 12 529-539 doi: 10.1016/s0007-1935(17)39028-0
Littlejohn A.No abstract available
Comparison of protein structure in the crystal and in solution. V. Solubility of horse methemoglobin and azide binding.
Journal of molecular biology    August 14, 1968   Volume 35, Issue 3 477-481 doi: 10.1016/s0022-2836(68)80007-5
Rupley JA, Gates V.No abstract available
Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: (1) x-ray analysis.
Nature    July 6, 1968   Volume 219, Issue 5149 29-32 doi: 10.1038/219029a0
Perutz MF, Miurhead H, Cox JM, Goaman LC, Mathews FS, McGandy EL, Webb LE.No abstract available
Structure and function of haemoglobin. IV. A three-dimensional Fourier synthesis of horse deoxyhaemoglobin at 5.5 A resolution.
Journal of molecular biology    April 14, 1968   Volume 33, Issue 1 283-297 doi: 10.1016/0022-2836(68)90294-5
Bolton W, Cox JM, Perutz MF.No abstract available
The reaction of carbon monoxide with horse hemoglobin in solution, in erythrocytes, and in crystals.
The Journal of biological chemistry    December 25, 1967   Volume 242, Issue 23 5762-5770 
Parkhurst LJ, Gibson QH.No abstract available
Identity of structure of horse deoxy- and oxyhaemoglobin after reaction with bis(N-maleidomethyl)ether.
Journal of molecular biology    September 28, 1967   Volume 28, Issue 3 451-454 doi: 10.1016/s0022-2836(67)80094-9
Simon SR, Konigsberg WH, Bolton W, Perutz MF.No abstract available
Immunological similarity of horse, donkey and mule haemoglobins.
Nature    August 5, 1967   Volume 215, Issue 5101 630-631 doi: 10.1038/215630a0
Cradock-Watson JE.No abstract available
Location of the heme in horse heart ferricytochrome c by x-ray diffraction.
The Journal of biological chemistry    June 25, 1967   Volume 242, Issue 12 3015-3018 
Dickerson RE, Kopka ML, Weinzierl J, Varnum J, Eisenberg D, Margoliash E.No abstract available
A comparison of the resistance of human and horse ferrihemoglobin to acid denaturation.
The Journal of biological chemistry    March 25, 1967   Volume 242, Issue 6 1294-1301 
Steinhardt J, Hiremath CB.Many of the stability characteristics of horse ferrihemo-globin (Hb+) in acid solutions, such as pH dependence and susceptibility to stabilization by iron ligands, are shared by human ferrihemoglobin, but striking differences between the two proteins exist. The most noticeable is the much greater rate of denaturation of the human protein at all pH values. Other differences include a shift to higher pH in the equi-librium between native and acid-denatured forms, differ-ences in the temperature at which the temperature effect on the equilibrium-pH curve reverses, a complete absence in human Hb+ ...
Studies of heme-proteins. I. Dissociation equilibria of horse hemoglobin.
Archives of biochemistry and biophysics    February 1, 1967   Volume 118, Issue 2 434-447 doi: 10.1016/0003-9861(67)90372-4
Mizukami H, Lumry R.No abstract available
Regulation of methaemoglobinaemia in horse and human erythrocytes.
The Australian journal of experimental biology and medical science    February 1, 1967   Volume 45, Issue 1 77-88 doi: 10.1038/icb.1967.4
Robin H, Harley JD.No abstract available
Amino-acid replacements in horse haemoglobin.
Nature    January 21, 1967   Volume 213, Issue 5073 269-271 doi: 10.1038/213269a0
Kilmartin JV, Clegg JB.No abstract available
[On the hemoglobin polymorphism in the zebra].
Zentralblatt fur Veterinarmedizin. Reihe A    January 1, 1967   Volume 14, Issue 1 91-92 
Schmid DO, Osterhoff DR.No abstract available
Genetic variation of horse hemoglobin.
Hereditas    January 1, 1967   Volume 58, Issue 3 385-392 doi: 10.1111/j.1601-5223.1967.tb02163.x
Braend M.No abstract available
Acid denaturation of horse carbonylhemoglobin in the absence of oxygen.
The Journal of biological chemistry    September 10, 1966   Volume 241, Issue 17 3988-3996 
Steinhardt J, Polet H, Moezie F.No abstract available
[Purification of horse spleen hemosiderin and its properties].
Seikagaku. The Journal of Japanese Biochemical Society    August 1, 1966   Volume 38, Issue 8 421-426 
Nakajima N, Muraoka T, Saito K, Watanabe T, Kuwabara M.No abstract available
[Study of the spiralization of hemoglobin by optical activity dispersion].
Biofizika    January 1, 1966   Volume 11, Issue 5 773-778 
Vol'kenshteĭn MV, Shemelin AK.No abstract available
Cell and Solution Velocity Constants for the Reaction CO + Hb –> COHb at Different Temperatures in Mammals with Different Red Cell Sizes.
The Journal of general physiology    November 1, 1965   Volume 49, Issue 2 199-220 doi: 10.1085/jgp.49.2.199
Holland RA.Using a double beam stopped-flow apparatus, measurements were made of the velocity constant of the reaction CO + Hb --> COHb in solution and in the red cells of human beings, rabbits, horses, and goats. The solution constant (l') at 37 degrees C for human beings was 362 mM(-1) sec.(-1); in other species l' was somewhat lower. Two rabbits, despite having apparently identical hemoglobins had significantly different values for l'. The energy of activation (E) of l' was between 8 and 11 kcal/mole in all cases. The cell reaction constant (l'(c)) at 37 degrees was between 61 and 73 mM(-1) sec.(-1...
Refractive index dispersion in equine hemoglobin solutions.
The Journal of physical chemistry    September 1, 1965   Volume 69, Issue 9 3188-3193 doi: 10.1021/j100893a513
Orttung WH, Warner J.No abstract available
[On hemoglobin polymorphism in the horse].
Zeitschrift fur Immunitatsforschung, Allergie und klinische Immunologie    June 1, 1965   Volume 128, Issue 5 499-503 
Schmid DO.No abstract available
The Evolution of Hemoglobin.
Scientific American    May 1, 1965   Volume 212 110-118 doi: 10.1038/scientificamerican0565-110
ZUCKERKANDL E.No abstract available
Molecular Orientation in Horse Hemoglobin Crystals and Sickled Erythrocytes.
Biochimica et biophysica acta    January 25, 1965   Volume 94 194-199 doi: 10.1016/0926-6585(65)90024-5
MURAYAMA M, OLSON RA, JENNINGS WH.No abstract available
[Oxidation of Horse Oxyhemoglobin by Sodium Nitrite].
Seikagaku. The Journal of Japanese Biochemical Society    January 1, 1965   Volume 37 14-20 
KAKIZAKI T, SATO M, TSURUTA H, HASEGAWA H.No abstract available
[Anomalous dispersion of the optical activity of dolphin myoglobin and horse hemoglobin].
Biokhimiia (Moscow, Russia)    January 1, 1965   Volume 30, Issue 1 148-152 
Vol'kenshteĭn MV, Shemelin AK.No abstract available
[Electronic Structure of the Prosthetic Groups and Tertiary Structure in Hemoproteins: I. Magnetic and Optical Properties of Divalent Horse Hemoglobin and Myoglobin under Reversible Detergent Action].
Journal of molecular biology    December 1, 1964   Volume 10 475-487 doi: 10.1016/s0022-2836(64)80067-x
GERSONDE K, NETTER H.No abstract available
The Immunochemical Difference Between Horse Oxy- and Deoxyhaemoglobin.
Journal of molecular biology    September 1, 1964   Volume 9 785-788 doi: 10.1016/s0022-2836(64)80184-4
REICHLIN M, BUCCI E, ANTONINI E, WYMAN J, ROSSI-FANELLI A.No abstract available
Structure of Hemoglobin: An X-Ray Examination of Reduced Horse Hemoglobin.
Nature    August 15, 1964   Volume 203 687-690 doi: 10.1038/203687a0
PERUTZ MF, BOLTON W, DIAMOND R, MUIRHEAD H, WATSON HC.No abstract available
Some Aspects of the Structure of Hemoglobin.
Canadian journal of biochemistry    May 1, 1964   Volume 42 755-762 doi: 10.1139/o64-087
SMITH DB.No abstract available
Influence of the Equine Spleen on Rapid Changes in the Concentration of Erythrocytes in Peripheral Blood.
American journal of veterinary research    March 1, 1964   Volume 25 500-504 
TORTEN M, SCHALM OW.No abstract available