Analyze Diet

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.
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
Primary structure of the alpha-chain from horse hemoglobin.
Journal of biochemistry    March 1, 1963   Volume 53 262-263 doi: 10.1093/oxfordjournals.jbchem.a127691
BRAUNITZER G, MATSUDA G.No abstract available
Differences in red-cell antigen strength in the horse due to gene interaction.
Nature    August 11, 1962   Volume 195 580-582 doi: 10.1038/195580a0
FRANKS D.No abstract available
Analogies and differences between human and horse haemoglobin.
Nature    August 4, 1962   Volume 195 507-508 doi: 10.1038/195507b0
MASIAR P.No abstract available
Horse blood groups and hemolytic disease of the newborn foal.
Annals of the New York Academy of Sciences    May 3, 1962   Volume 97 235-250 doi: 10.1111/j.1749-6632.1962.tb34639.x
FRANKS D.No abstract available
[Preparation of rabbit haptoglobin and horse haptoglobin].
Comptes rendus hebdomadaires des seances de l'Academie des sciences    February 19, 1962   Volume 254 1525-1526 
MARNAY A, JAYLE MF.No abstract available
[On the effect of hydrogen ion concentration and SH reagents on the redox potential of hemin, equine myoglobin and different hemoglobins].
Acta biologica et medica Germanica    January 1, 1962   Volume 8 88-102 
BEHLKE J, SCHELER W.No abstract available
[The neutral fraction of low molecular weight pepsin-peptides of equine hemoglobin].
Biokhimiia (Moscow, Russia)    May 1, 1961   Volume 26 462-467 
OPPEL' VV.No abstract available
The reaction of sulphuric acid with lysozyme and horse globin.
Canadian journal of biochemistry and physiology    January 1, 1961   Volume 39 31-43 doi: 10.1139/o61-005
HABEEB AF.No abstract available
Dissociation of horse hemoglobin at high pH.
Archives of biochemistry and biophysics    June 1, 1960   Volume 88 298-301 doi: 10.1016/0003-9861(60)90239-3
KURIHARA K, SHIBATA K.No abstract available
The amino acid contents of horse globin and of its component polypeptides.
Canadian journal of biochemistry and physiology    March 1, 1960   Volume 38 263-268 
HABEEB AF, SMITH DB.Horse globill and its conlponent polypeptide chains obtained by fractional precipitation and column chroinatography have been ailalyzed for their con- stituent amino acids. The principal difference between the two chains is that the valyl-leucyl chain is rich in serine and threonine and poor in glutamic acid and tryptophan compared to the \-alyl-glutaininyl chain.