Analyze Diet

Topic:Biology

The study of biology in horses encompasses the examination of their physiological, genetic, and cellular processes. This field investigates the anatomical structures, reproductive biology, and genetic makeup of horses, offering insights into their growth, development, and adaptation. Researchers focus on various aspects such as equine genetics, which explores hereditary traits and genetic disorders, and equine physiology, which examines the functions of different systems within the horse's body, including the cardiovascular, respiratory, and musculoskeletal systems. This page assembles peer-reviewed research studies and scholarly articles that explore the biological mechanisms and processes in horses, providing a comprehensive understanding of their biological functions and health.
Coprophagy in animals: a review.
The Cornell veterinarian    October 1, 1991   Volume 81, Issue 4 357-364 
Soave O, Brand CD.Coprophagy is performed by rodents and lagomorphs and to a lesser degree by piglets, foals, dogs and nonhuman primates. Due to the construction of the digestive system of rodents and rabbits, coprophagy is necessary to supply many essential nutrients. Bacterial synthesis of nutrients occurs in the lower gastrointestinal tract in these animals where little absorption is realized. The eating of their feces provides a method for obtaining these nutrients.
Genomic distribution of heterochromatic sequences in equids: implications to rapid chromosomal evolution.
The Journal of heredity    September 1, 1991   Volume 82, Issue 5 369-377 doi: 10.1093/oxfordjournals.jhered.a111106
Wichman HA, Payne CT, Ryder OA, Hamilton MJ, Maltbie M, Baker RJ.We describe a molecular model for rapid chromosomal evolution that proposes tandemly repeated DNA sequences as a driving force. A prediction of this model is that when extensive rearrangements of euchromatin have been facilitated by heterochromatin, genomes will be characterized by tandemly repeated sequences that have actively changed chromosomal fields by intragenomic movement. Alternatively, it is proposed that in conservative chromosomal lineage each class of tandemly repeated sequences will be restricted to a specific chromosomal field. To provide baseline data to test this model we exami...
1H NMR resonance assignments in a paramagnetic heme protein by two-dimensional spectroscopy: heme resonances in equine met-azido myoglobin.
Biochemical and biophysical research communications    March 15, 1991   Volume 175, Issue 2 515-519 doi: 10.1016/0006-291x(91)91594-3
Peyton DH.Specific heme protons for the majority of resonances in the downfield resolved region of equine met-azido myoglobin have been assigned using solely the two-dimensional 1H NMR experiments NOESY and COSY. Metazido myoglobin provides a useful test case for the applicability of these techniques to paramagnetic proteins for the following reasons. First met-azido myoglobin is a mixed spin-state protein, with significantly shorter relaxation times and broadened lines relative to pure low-spin systems (eg., met-cyano myoglobin). Second, met-azido hemoglobin and met-azido myoglobin are important as mod...
Beta-subunits of equine chorionic gonadotropin and lutenizing hormone with an identical amino acid sequence have different asparagine-linked oligosaccharide chains.
Biochemical and biophysical research communications    January 31, 1991   Volume 174, Issue 2 940-945 doi: 10.1016/0006-291x(91)91509-b
Matsui T, Sugino H, Miura M, Bousfield GR, Ward DN, Titani K, Mizuochi T.The glycoprotein hormones, equine chorionic gonadotropin (eCG) and lutenizing hormone (eLH), possess a beta-subunit with an identical amino acid sequence. The Asn-linked oligosaccharide chains of eCG beta and eLH beta were quantitatively liberated as tritium-labeled oligosaccharides by hydrazinolysis followed by N-acetylation and NaB3H4-reduction. Paper electrophoresis in combination with sialidase digestion and solvolytic desulfation indicated that eCG beta contained neutral and sialylated oligosaccharides, while eLH beta contained neutral, sialylated, sulfated, and both sialylated and sulfat...
Inheritance of the equine Tf F3 allele.
Animal genetics    January 1, 1991   Volume 22, Issue 2 187-190 doi: 10.1111/j.1365-2052.1991.tb00662.x
Cothran EG, Henney PJ, King JA.The inheritance of the equine Tf F3 allele was examined in 39 parent-offspring combinations. For 26 of the cases the allele inherited by the offspring from the heterozygous parent could be determined. The proportion of individuals that inherited the F3 variant compared to the alternative allele was exactly 1:1. In five cases the parental phenotype was identical to that of the offspring. For the remaining eight cases the parent was homozygous for the F3 allele and all offspring had the F3 allele. The results were consistent with Mendelian inheritance.
Mechanisms of sodium and chloride transport across equine tracheal epithelium.
The American journal of physiology    December 1, 1990   Volume 259, Issue 6 Pt 1 L459-L467 doi: 10.1152/ajplung.1990.259.6.L459
Tessier GJ, Traynor TR, Kannan MS, O'Grady SM.Equine tracheal epithelium, stripped of serosal muscle, mounted in Ussing chambers, and bathed in plasmalike Ringer solution generates a serosa-positive transepithelial potential of 10-22 mV and a short-circuit current (Isc) of 70-200 microA/cm2. Mucosal amiloride (10 microM) causes a 40-60% decrease in Isc and inhibits the net transepithelial Na flux by 95%. Substitution of Cl with gluconate resulted in a 30% decrease in basal Isc. Bicarbonate substitution with 20 mM N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid decreased the Isc by 21%. The Cl-dependent Isc was inhibited by serosal add...
The carbohydrate side chains of the major plasma serpins of horse and wallaby: analyses of enzymatic and chemically treated (including ‘Smith degradation’) protein blots by lectin binding.
Biochemistry international    January 1, 1990   Volume 20, Issue 3 429-436 
Patterson SD, Bell K.The carbohydrate side chains of the major plasma serpins of the horse and wallaby have been characterized by lectin analyses of protein blots from two-dimensional gels using the major human plasma serpin, alpha 1-protease inhibitor, as a control. Eight lectins were used in the characterization in conjunction with enzymatic deglycosylation of complex and high mannose side chains, chemical desialylation and defucosylation, and one round of 'Smith degradation', all being performed on the nitrocellulose blots. Assuming a standard complex side chain structure, the results of the 21 lectin/treatment...
Transbilayer movement of phosphatidylserine in nonhuman erythrocytes: evidence that the aminophospholipid transporter is a ubiquitous membrane protein.
Biochemistry    December 12, 1989   Volume 28, Issue 25 9680-9685 doi: 10.1021/bi00451a021
Connor J, Schroit AJ.A 31-32-kDa integral membrane protein has been previously identified in erythrocytes as the protein most likely to be responsible for the transbilayer movement of phosphatidylserine (PS) [Connor & Schroit (1988) Biochemistry 27, 848-851]. Using similar techniques, we have identified analogous proteins of identical molecular weights in bovine, equine, ovine, porcine, canine, caprine, and rhesus red blood cells. Similar to human red blood cells, all of the mammalian cells were able to specifically transport an exogenously supplied fluorescent PS analogue from their outer-to-inner membrane le...
Differential transport of fertilised and unfertilised eggs in equine fallopian tubes: a straightforward explanation.
The Veterinary record    September 9, 1989   Volume 125, Issue 11 304 doi: 10.1136/vr.125.11.304
Hunter RH.No abstract available
Comparison of partial amino acid sequences of two protamine 2 variants from stallion sperm. Structural evidence that the variants are products of different genes.
FEBS letters    February 13, 1989   Volume 244, Issue 1 199-202 doi: 10.1016/0014-5793(89)81192-5
Pirhonen A, Linnala-Kankkunen A, Mäenpää PH.Protamine 1 and two protamine 2 variants were isolated from stallion sperm and separated by acetic acid-urea gel electrophoresis. After electroblotting onto polyvinyldifluoride filters, their amino-terminal amino acid sequences were determined by pulse-liquid peptide sequencing. The sequences of the two protamine 2 variants are homologous but slightly different in length and amino acid composition and indicate for the first time the existence of two different genes for this protamine species.
Localization of the equine major histocompatibility complex (ELA) to chromosome 20 by in situ hybridization.
Hereditas    January 1, 1989   Volume 110, Issue 1 93-96 doi: 10.1111/j.1601-5223.1989.tb00425.x
Mäkinen A, Chowdhary B, Mahdy E, Andersson L, Gustavsson I.No abstract available
Prolactin receptors in the choroid plexus of non-mammalian and mammalian species.
Pharmacological research    January 1, 1989   Volume 21, Issue 1 95-96 doi: 10.1016/1043-6618(89)90130-8
Muccioli G, Papotti M, Di Carlo R, Genazzani E.No abstract available
Comparative anatomy of the accessory ciliary ganglion in mammals.
Anatomy and embryology    January 1, 1989   Volume 180, Issue 2 199-205 doi: 10.1007/BF00309772
Kuchiiwa S, Kuchiiwa T, Suzuki T.The orbits of 13 mammalian species (pig, sika deer, domestic sheep, horse, cat, fox, racoon dog, marten, rat, rabbit, crab-eating macaque, japanese macaque and man) were stained with silver nitrate and dissected under a dissecting microscope with special attention to the presence and location of the accessory ciliary ganglion. Some preparations were stained with thionin and examined as whole-mounts in a transmission microscope. The accessory ciliary ganglion was present in all 13 species, although the number and degree of development varied greatly from species to species. The accessory ciliar...
Evolution of tooth structure in the Equoidea.
The Journal of Nihon University School of Dentistry    December 1, 1988   Volume 30, Issue 4 287-296 doi: 10.2334/josnusd1959.30.287
Kozawa Y, Mishima H, Sakae T.During the evolution of the Equoidea, the histological structures of the teeth have become more complex as the molars have become hypsodont in form. The straight Hunter-Schreger bands of Hiracotherium have evolved into a more complex pattern in Equus. The enamel prisms changed from an arched form (about 5μm in diameter) with an alternating pattern in Hiracotherium to an oval form (about 2 μm width) arranged in straight rows in Equus. In Equus the rows of prisms are separated by interprismatic sheets. This pattern may have increased the architectural strength of the enamel, and is related to ...
Mechanism of binding of horse liver alcohol dehydrogenase and nicotinamide adenine dinucleotide.
Biochemistry    July 12, 1988   Volume 27, Issue 14 5082-5088 doi: 10.1021/bi00414a020
Sekhar VC, Plapp BV.The binding of NAD+ to liver alcohol dehydrogenase was studied by stopped-flow techniques in the pH range from 6.1 to 10.9 at 25 degrees C. Varying the concentrations of NAD+ and a substrate analogue used to trap the enzyme-NAD+ complex gave saturation kinetics. The same maximum rate constants were obtained with or without the trapping agent and by following the reaction with protein fluorescence or absorbance of a ternary complex. The data fit a mechanism with diffusion-controlled association of enzyme and NAD+, followed by an isomerization with a forward rate constant of 500 s-1 at pH 8: E E...
Epidermal cell renewal in the horse.
American journal of veterinary research    April 1, 1988   Volume 49, Issue 4 520-521 
Barker BB, Stannard AA, Maibach HI.Epidermal cell labeling index and cell renewal time were estimated in 8 adult horses, using autoradiography after [3H]thymidine was given intradermally. The mean labeling index was 1.45 +/- 0.47%, and the mean cell renewal time of the viable epidermis was approximately 17 days.
Sex chromosomes of horses; or what the X happening?
Equine veterinary journal    March 1, 1988   Volume 20, Issue 2 81-82 doi: 10.1111/j.2042-3306.1988.tb01461.x
Gill JJ.No abstract available
Comparative scanning electron-microscopic study of the lingual papillae in two species of domestic mammals (Equus caballus and Bos taurus). II. Mechanical papillae.
Acta anatomica    January 1, 1988   Volume 132, Issue 2 120-123 
de Paz Cabello P, Chamorro CA, Sandoval J, Fernandez M.The mechanical papillae of the horse and cow were studied by scanning electron microscopy in order to determine their morphostructural characteristics and the differences between the two species. The horse has only thin, small and interlaced filiform papillae, while the cow shows robust and more ordered filiform papillae. Furthermore, the cow tongue presents conical and lenticular papillae surrounded by a papillary groove. A characteristic distribution of stratified scales and channeled tracts is observed in conical and lenticular papillae but not in the filiform papillae. The morphostructural...
Heterogeneity of amino acid transport in horse erythrocytes: a detailed kinetic analysis of inherited transport variation.
The Journal of physiology    August 1, 1987   Volume 389 385-409 doi: 10.1113/jphysiol.1987.sp016662
Fincham DA, Mason DK, Paterson JY, Young JD.1. Thoroughbred horses were divisible into five distinct amino acid transport subgroups on the basis of their erythrocyte permeability to L-alanine, measured uptake rates ranging from 5 to 625 mumol l cells-1 h-1 (0.2 mM-extracellular L-alanine, 37 degrees C). 2. Erythrocytes from animals belonging to the lowest L-alanine permeability subgroup (5-15 mumol l cells-1 h-1) (transport-deficient type) exhibited slow nonsaturable transport of this amino acid. In contrast, cells from horses of the four transport-positive subgroups possessed additional high-affinity (apparent L-alanine Km (Michaelis c...
[Tolerance of Wellcare emulsion by horses with special reference to red blood cell formation and locomotion].
DTW. Deutsche tierarztliche Wochenschrift    July 1, 1987   Volume 94, Issue 7 385-391 
Andresen U, Pavel G.No abstract available
A soluble class I molecule analogous to mouse Q10 in the horse and related species.
Immunogenetics    January 1, 1986   Volume 23, Issue 5 277-283 doi: 10.1007/BF00398789
Lew AM, Valas RB, Maloy WL, Coligan JE.Horse serum is shown to contain a soluble class I molecule analogous to the secreted Q10 molecule in the mouse. This molecule has several similarities to the recently described mouse Q10 molecule: it is smaller than membrane-bound equine class I molecules; it occurs in a high molecular mass complex of 200-300 kd in serum; and the serum levels of the equine molecule are similar to that of the Q10 molecule (about 30 micrograms/ml). A soluble molecule is also detected in the sera of species related to the horse; it has in fact been found in all the wild members of the order Perissodactyla so far ...
Limits to exercise performance: some ideas from comparative studies.
Acta physiologica Scandinavica. Supplementum    January 1, 1986   Volume 556 45-51 
Elsner R.Examples of exercise performance and metabolic scope in non-human mammalian species are considered from the point of view of problems and questions which may provide insights into evolutionary processes influencing adaptations to muscular activity. Consideration of both aerobic and anaerobic performance is required. Some recent approaches, notably that concerned with the concept of symmorphosis, the integration of design for the accommodation of variations in activity, show promise of new ways for comparative investigations of the adjustments to exercise.
Kinetic studies of the unfolding-refolding of horse muscle phosphoglycerate kinase induced by guanidine hydrochloride.
Biochemistry    August 13, 1985   Volume 24, Issue 17 4570-4577 doi: 10.1021/bi00338a013
Betton JM, Desmadril M, Mitraki A, Yon JM.The kinetics of the unfolding and refolding of horse muscle phosphoglycerate kinase were studied with three different signals: fluorescence emission intensity at 336 nm (excitation at 292 nm), ellipticity at 220 nm, and enzyme activity. The results corroborate the conclusion on the existence of intermediates in the folding pathway obtained from equilibrium studies. Kinetic studies showed at least two phases of refolding, as revealed by fluorescence as well as by circular dichroism measurements. During the fast phase, an intermediate was formed with a fluorescence intensity higher than that of ...
[Isolation and properties of a nonspecific adhesive factor from the blood serum of warm-blooded animals and man].
Zhurnal obshchei biologii    May 1, 1985   Volume 46, Issue 3 389-400 
Reznikova MM, Iamskova VP.No abstract available
Iron deposition in apoferritin. Evidence for the formation of a mixed valence binuclear iron complex.
The Journal of biological chemistry    March 10, 1985   Volume 260, Issue 5 2926-2929 
Chasteen ND, Antanaitis BC, Aisen P.A preliminary EPR investigation of iron accumulation in apoferritin has identified paramagnetic species generated during the early stage of iron deposition within the apoprotein shell. A featureless resonance at g' = 4.3, attributable to solitary high spin Fe3+ ions bound to the protein, is generated when Fe(II) is added to apoferritin at a level of 0.5 Fe/subunit (12 Fe/molecule) followed by air oxidation. This resonance accounts for 36% of the added iron. The remainder is EPR-silent and is probably present as oligomeric Fe3+ species. The intensity of the g' = 4.3 signal is reduced 3-fold upo...
In utero nature versus nurture.
Equine veterinary journal    March 1, 1985   Volume 17, Issue 2 97-98 doi: 10.1111/j.2042-3306.1985.tb02058.x
Woollam DH.No abstract available
Development of the digestive system: comparative animal studies.
The American journal of clinical nutrition    February 1, 1985   Volume 41, Issue 2 Suppl 384-390 doi: 10.1093/ajcn/41.2.384
Widdowson EM.No abstract available
The amino acid sequence of equine alpha-lactalbumin.
Biochemistry international    November 1, 1984   Volume 9, Issue 5 539-546 
Kaminogawa S, McKenzie HA, Shaw DC.The amino acid sequence of equine alpha-lactalbumin has been determined with the aid of an automatic sequencer. The protein chain consists of 123 amino acids and has a Mr of 14218. Elucidation of the structure involved sequence determination of native protein (residues 1-32), cyanogen bromide fragments, and tryptic, chymotryptic and S. aureus V8 proteolytic peptides. Approximately 67% of the residues are identical with corresponding residues of bovine alpha-lactalbumin B, and there is close homology with alpha-lactalbumin of other species.
Invasive trophoblast in the genus Equus.
Annales d'immunologie    November 1, 1984   Volume 135D, Issue 3 325-331 doi: 10.1016/s0769-2625(84)81201-5
Antczak DF, Allen WR.No abstract available
[The biology of Eimeria leuckarti (Flesch, 1883) in Equidae].
Berliner und Munchener tierarztliche Wochenschrift    October 1, 1984   Volume 97, Issue 10 367-372 
Bauer C, Bürger HJ.No abstract available