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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.
The autoxidation of horse hemoglobin: the effect of glutathione.
Biochimica et biophysica acta    June 26, 1972   Volume 273, Issue 1 30-39 doi: 10.1016/0304-4165(72)90188-2
Rifkind JM.The reduced glutathione in the erythrocyte was found to inhibit the autoxidation of purified horse hemoglobin. It was observed that much higher concentrations of oxidized glutathione also stabilize hemoglobin. The stabilization by oxidized glutathione most likely involves the formation of a mixed disulfide with the reactive β-93 sulfhydryl groups on the hemoglobin. A similar effect is also observed with N-ethyl- maleimide and HgCl2 which also react with the sulfhydryl groups. The apparent stabilization by reduced glutathione is partially due to the reduction of ferrihemoglobin formed by autox...
Distribution of erythrocyte carbonic anhydrase B-type alleles in Japanese farm horses.
Biochemical genetics    June 1, 1972   Volume 6, Issue 4 255-262 doi: 10.1007/BF00486119
Deutsch HF, Taniguchi N, Funakoshi S, Hirai H.No abstract available
Titration behavior of histidines in human, horse, and bovine hemoglobins.
The Journal of biological chemistry    March 25, 1972   Volume 247, Issue 6 1743-1749 
Janssen LH, de Bruin SH, van Os GA.No abstract available
Equine bacillary hemoglobinuria (a case report).
Veterinary medicine, small animal clinician : VM, SAC    March 1, 1972   Volume 67, Issue 3 279-283 
Kirk MD.No abstract available
Acute hemolytic anemia caused by wild onion poisoning in horses.
Journal of the American Veterinary Medical Association    February 1, 1972   Volume 160, Issue 3 323-327 
Pierce KR, Joyce JR, England RB, Jones LP.No abstract available
[Structural components of the erythrocyte membrane].
Postepy biochemii    January 1, 1972   Volume 18, Issue 3 351-373 
Gondko R, Slomiany B, Slaska K.No abstract available
Hematopoietic response to hematinics in horses.
Journal of the American Veterinary Medical Association    December 1, 1971   Volume 159, Issue 11 1316-1318 
Kirkham WW, Guttridge H, Bowden J, Edds GT.No abstract available
Effects of a piperazine-carbon disulfide-phenothiazine preparation on hemoglobin and packed cell values of horses.
Journal of the American Veterinary Medical Association    November 1, 1971   Volume 159, Issue 10 1260-1262 
Blevins DI, Miller CC, Kleckner MD.No abstract available
The binding of carbon dioxide by horse haemoglobin.
The Biochemical journal    August 1, 1971   Volume 124, Issue 1 31-45 doi: 10.1042/bj1240031
Kilmartin JV, Rossi-Bernardi L.1. Three modified horse haemoglobins have been prepared: (i) alpha(c) (2)beta(c) (2), in which both the alpha-amino groups of the alpha- and beta-chains have reacted with cyanate, (ii) alpha(c) (2)beta(2), in which the alpha-amino groups of the alpha-chains have reacted with cyanate, and (iii) alpha(2)beta(c) (2), in which the two alpha-amino groups of the beta-chain have reacted with cyanate. 2. The values of n (the Hill constant) for alpha(c) (2)beta(c) (2), alpha(2)beta(c) (2) and alpha(c) (2)beta(2) were (respectively) 2.5, 2.0 and 2.6, indicating the presence of co-operative interactions ...
Haptoglobins in the horse.
The Veterinary record    July 24, 1971   Volume 89, Issue 4 106-109 doi: 10.1136/vr.89.4.106
Allen B, Archer RK.No abstract available
Effect of age on erythrogram values of thoroughbred horses from 1 to 12 months of age.
Zentralblatt fur Veterinarmedizin. Reihe A    July 1, 1971   Volume 18, Issue 5 395-400 doi: 10.1111/j.1439-0442.1971.tb00592.x
Medeiros LO, Martins LF, Ferri S, Barcelos SR.No abstract available
Influence of chemical modifications of the reactive SH groups on the proton binding behaviour of human and horse hemoglobin.
Biochimica et biophysica acta    June 29, 1971   Volume 236, Issue 3 777-779 doi: 10.1016/0005-2795(71)90262-5
Janssen LH, de Bruin SH, van OS GA.No abstract available
Structure and functional properties of chemically modified horse hemoglobin. I. Determination of the functional properties.
Journal of molecular biology    May 28, 1971   Volume 58, Issue 1 69-77 doi: 10.1016/0022-2836(71)90232-4
Simon SR, Arndt DJ, Konigsberg WH.No abstract available
Structure and functional properties of chemically modified horse hemoglobin. II. X-ray studies.
Journal of molecular biology    May 28, 1971   Volume 58, Issue 1 79-88 doi: 10.1016/0022-2836(71)90233-6
Moffat JK.No abstract available
Free erythrocyte protoporphyrin in the horse.
Research in veterinary science    May 1, 1971   Volume 12, Issue 3 280-282 
Barnett AL, Steel JD, Stewart GA.Free erythrocyte protoporphyrin was estimated in 166 Thoroughbred horses and the mean value was found to be 4o vg.Poo ml. packed cells. Signifi-cantly lower haemoglobin concentrations were found in 21 horses whose erythrocyte protoporphyrin concentration was 7o p.g.lioo ml. packed cells or greater.
[Levels of 2,3 diphosphoglycerate in erythrocytes of mammals].
Archivos del Instituto de Biologia Andina    May 1, 1971   Volume 4, Issue 2 67-73 
Reynafarje B, Rosenmann M.No abstract available
Three dimensional fourier synthesis of horse deoxyhaemoglobin at 2.8 Angstrom units resolution.
Nature    November 7, 1970   Volume 228, Issue 5271 551-552 doi: 10.1038/228551a0
Bolton W, Perutz MF.No abstract available
Horse haemoglobin polymorphism: evidence for two linked non-allelic alpha-chain genes.
Proceedings of the Royal Society of London. Series B, Biological sciences    November 3, 1970   Volume 176, Issue 1043 235-246 doi: 10.1098/rspb.1970.0041
Clegg JB.No abstract available
Stabilization of horse globin by protoporphyrin IX and hemin.
The Journal of biological chemistry    October 25, 1970   Volume 245, Issue 20 5395-5403 
Sebring ED, Steinhardt J.No abstract available
Equine infectious anaemia: the role of Heinz bodies in the pathogenesis of anaemia.
Research in veterinary science    July 1, 1970   Volume 11, Issue 4 354-357 
McGuire TC, Henson JB, Keown GH.No abstract available
[Hemoglobin concentration, oxygen saturation and oxygen content of the blood in breeding and sport horses during various stages of training].
Berliner und Munchener tierarztliche Wochenschrift    June 15, 1970   Volume 83, Issue 12 229-234 
von Engelhardt W, Ehrlein HJ, Hörnicke H.No abstract available
Gene expression in an interspecific hybrid: analysis of hemoglobins in donkey, horse, and mule by peptide mapping.
Biochemical genetics    February 1, 1970   Volume 4, Issue 1 73-85 doi: 10.1007/BF00484019
Isaacs WA.No abstract available
[pH-dependency of circular dichroism of human and cattle hemoglobin and horse myoglobin].
Acta biologica et medica Germanica    January 1, 1970   Volume 24, Issue 1 25-32 
Ruckpaul K, Grill H, Jung F.No abstract available
Comparison of the resistance of human and horse ferrihemoglobin ligand derivatives to acid denaturation.
Biochimica et biophysica acta    December 23, 1969   Volume 194, Issue 2 364-375 doi: 10.1016/0005-2795(69)90097-x
Molday RS, Steinhardt J.No abstract available
Structural comparison of the hemoglobins of the genus Equus with those of ruminants.
The Journal of biological chemistry    December 10, 1969   Volume 244, Issue 23 6533-6542 
Kitchen H, Easley CW.No abstract available
Heterogeneity of erythrocyte catalase. Correlations between sulfhydryl group content, chromatographic and electrophoretic properties.
European journal of biochemistry    November 1, 1969   Volume 11, Issue 1 49-57 doi: 10.1111/j.1432-1033.1969.tb00737.x
Mörikofer-Zwez S, Cantz M, Kaufmann H, von Wartburg JP, Aebi H.No abstract available
Rate of O2 dissociation from O2Hb and relative combination rate of CO and O2 in mammals at 37 degrees C.
Respiration physiology    June 1, 1969   Volume 7, Issue 1 30-42 doi: 10.1016/0034-5687(69)90067-x
Holland RA.No abstract available
Rate at which CO replaces O2 from O2Hb in red cells of different species.
Respiration physiology    June 1, 1969   Volume 7, Issue 1 43-63 doi: 10.1016/0034-5687(69)90068-1
Holland RA.No abstract available
Measurement of ligand-induced conformational changes in hemoglobin by circular dichroism.
Proceedings of the National Academy of Sciences of the United States of America    May 1, 1969   Volume 63, Issue 1 205-212 doi: 10.1073/pnas.63.1.205
Simon SR, Cantor CR.The UV circular-dichroism spectra of human and horse hemoglobins have been determined at various degrees of partial saturation with oxygen. Spectra of the two native hemoglobins were compared with spectra of the corresponding proteins modified with a reagent known to eliminate the conformational rearrangement normally associated with cooperativity. Such comparison indicates that one region, around 260 mmu, is sensitive chiefly to the state of the hemes; changes in another region, around 285 mmu, may be correlated with the conformational transformation linked to cooperative interactions. All ci...
Hemogram of the Arabian horse.
American journal of veterinary research    February 1, 1969   Volume 30, Issue 2 295-298 
Knill LM, McConaughy C, Camarena I, Day M.No abstract available