Analyze Diet

Topic:Kinetics

Kinetics in horses refers to the study of motion and the forces that produce or alter such motion in equine subjects. This area of research involves analyzing the movement patterns of horses to understand the mechanics of locomotion, including gait analysis, stride length, and joint angles. Kinetic studies often employ tools such as force plates and motion capture systems to quantify the forces exerted by and upon the horse during various activities. These studies provide insights into the efficiency and biomechanics of equine movement, contributing to fields such as veterinary medicine, sports science, and rehabilitation. This page compiles peer-reviewed research studies and scholarly articles that explore the principles, methodologies, and applications of kinetic analysis in horses.
Rapid-scanning spectral evidence for catalytically nonequivalent but interconvertible forms of equine liver alcohol dehydrogenase.
Biochimie    February 1, 1981   Volume 63, Issue 2 97-102 doi: 10.1016/s0300-9084(81)80171-x
Koerber SC, Dunn MF.These rapid-scanning stopped-flow kinetic studies of the equine liver alcohol dehydrogenase-catalyzed reduction of p-nitrobenzaldehyde by NADH and (4R)-4-deuterio NADH (NADD) under single turnover conditions establish : (1) The reaction is biphasic using NADD as coenzyme, k1 approximately 200 sec-1, k2 = 0.5 sec-1 and the amplitude ratio (A1)/(A1 + A2) approximately equal to 0.5. (2) Each phase of the reaction involves the oxidation of enzyme-bound reduced coenzyme. (3) The recycling of sites in the presence of 20 mM pyrazole is negligible. (4) The rates of E(NAD-pyrazole) complex formation at...
Comparison of yeast and beef cytochrome c oxidases. Kinetics and binding of horse, fungal, and Euglena cytochromes c.
The Journal of biological chemistry    December 10, 1979   Volume 254, Issue 23 11973-11981 
Dethmers JK, Ferguson-Miller S, Margoliash E.No abstract available
Kinetics of gonadotrophins in the mare.
Journal of reproduction and fertility. Supplement    January 1, 1979   Issue 27 131-141 
Irvine CH.Isoelectric focussing of crude extracts of equine pituitaries was used to obtain fractions containing FSH and LH. By comparison with FSH, LH was distributed over a similar but wider pH range indicating more marked polymorphism as determined from their isoelectric point (pI). Molecules with more sialic acid showed lower pI consistent with the concept that sialic acid is the major factor in determining pI and polymorphism in FSH and LH. Appropriate fractions were labelled with 125I, purified further and used in kinetic studies. FSH and LH molecules of similar pI had similar kinetics; however, LH...
Stability and kinetic behavior of carboxymethylated horse muscle acylphosphatase.
Physiological chemistry and physics    January 1, 1978   Volume 10, Issue 4 367-373 
Stefani M, Berti A, Camici G, Manao G, Cappugi G, Ramponi G.Horse muscle acylphosphatase consists of a main chain S-S bound to glutathione. It was found that removal of the glutathione by reduction and successive carboxymethylation of the only cysteine of the main chain affects the stability of the enzyme, mainly with respect to thermal inactivation. On the other hand, the kinetic properties of the enzyme are affected very little.
Electron-transfer protein reactivities. Kinetic studies of the oxidation of horse heart cytochrome c, Chromatium vinosum high potential iron-sulfur protein, Pseudomonas aeruginosa azurin, bean plastocyanin, and Rhus vernicifera stellacyanin by pentaamminepyridineruthenium(III).
Journal of the American Chemical Society    July 20, 1977   Volume 99, Issue 15 5158-5167 doi: 10.1021/ja00457a042
Cummins D, Gray HB.No abstract available
Exercise studies in horses: 2. The cardiac response to exercise in normal horses and in horses with chronic obstructive pulmonary disease.
Equine veterinary journal    April 1, 1977   Volume 9, Issue 2 75-83 doi: 10.1111/j.2042-3306.1977.tb03986.x
Littlejohn A, Kruger JM, Bowles F.The relationship of velocity (v) to heart rate (HR)and of kinetic energy (KE) to heart rate, were investigated in 6 normal horses and in 6 horses with chronic obstructive pulmonary, disease (COPD). Radiotelemetry was used to determine the heart rate while subjects were ridden on a 400m track. Velocity was measured by stop-watch between 2 markers 50 m apart at the end of the track. Kinetic energy was calculated from the formula KE =1/2 Mv2, where M = mass of horse, rider, saddle and bridle (KG) and V = velocity (metres per second). In all subjects, the relationship of velocity to heart rate was...
Steady state kinetics and binding of eukaryotic cytochromes c with yeast cytochrome c peroxidase.
The Journal of biological chemistry    February 10, 1977   Volume 252, Issue 3 919-926 
Kang CH, Ferguson-Miller S, Margoliash E.1. The steady state kinetics for the oxidation of ferrocytochrome c by yeast cytochrome c peroxidase are biphasic under most conditions. The same biphasic kinetics were observed for yeast iso-1, yeast iso-2, horse, tuna, and cicada cytochromes c. On changing ionic strength, buffer anions, and pH, the apparent Km values for the initial phase (Km1) varied relatively little while the corresponding apparent maximal velocities varied over a much larger range. 2. The highest apparent Vmax1 for horse cytochrome c is attained at relatively low pH (congruent to 6.0) and low ionic strength (congruent to...
The purification and kinetic properties of biophosphoglycerate synthase from horse red blood cells.
Archives of biochemistry and biophysics    November 1, 1976   Volume 177, Issue 1 284-292 doi: 10.1016/0003-9861(76)90438-0
Rose AB, Dube S.No abstract available
Kinetics of the hydrolysis of synthetic substrates by horse urinary kallikrein and trypsin.
General pharmacology    August 1, 1976   Volume 7, Issue 2-3 167-171 doi: 10.1016/0306-3623(76)90056-2
Sampaio MU, Galembeck F, Paiva AC, Prado ES.The kinetic constants for horse urinary kallikrein and trypsin hydrolysis of BAEE, TAME, bradykinin methyl ester and bradykinyl-Ser-Val-Gin-Val-Ser were determined. The values of the ratio kcat/Km show that (1) kallikrein is catalytically less efficient than trypsin for all the substrates (2) the three esters are equally good substrates for trypsin while horse urinary kallikrein is 100-fold more effective on bradykinin methyl ester than on the other substrates (3) for both enzymes the ester of bradykinin is a better substrate than the tetradecapeptide.
Mammalian erythrocyte glutathione reductase: kinetic constants and saturation with cofactor.
American journal of veterinary research    October 1, 1975   Volume 36, Issue 10 1511-1513 
Harvey JW, Kaneko JJ.Glutathione reductase (GR) was studied in erythrocytes of horses, cats, dogs, and man. Glutathione reductase activity was measured in hemolysates with and without preincubation of hemolysates with flavinadenine dinucleotide. The percentage saturation of GR apoenzyme with cofactor (flavin-adenine dinucleotide) was lower in cats and dogs than in horses or man. The greatest amount of inactive apoenzyme was in feline erythrocytes. Total GR activity listed in order by species is cat greater than man greater than dog greater than horse. Kinetic constants for oxidized glutathione and reduced nicotina...
Horse liver alcohol dehydrogenase. A study of the essential lysine residue.
The Biochemical journal    September 1, 1975   Volume 149, Issue 3 627-635 doi: 10.1042/bj1490627
Chen SS, Engel PC.1. The inactivation of horse liver alcohol dehydrogenase by pyridoxal 5'-phosphate in phosphate buffer, pH8, at 10 degrees C was investigated. Activity declines to a minimum value determined by the pyridoxal 5'-phosphate concentration. The maximum inactivation in a single treatment is 75%. This limit appears to be set by the ratio of the first-order rate constants for interconversion of inactive covalently modified enzyme and a readily dissociable non-covalent enzyme-modifier complex. 2. Reactivation was virtually complete on 150-fold dilution: first-order analysis yielded an estimate of the r...
An examination of octanol and octanal metabolism to octanoic acid by horse liver alcohol dehydrogenase.
Biochimica et biophysica acta    March 28, 1975   Volume 384, Issue 1 1-11 doi: 10.1016/0005-2744(75)90090-x
Hinson JA, Neal RA.The kinetics of the horse liver alcohol dehydrogenase (alcohol: NAD+ oxidoreductase EC 1.1.1.1) catalyzed metabolism of octanol and octanal to octanoic acid have been examined. On incubation of octanol with horse liver alcohol dehydrogenase in the presence of NAD+, NADH as well as octanal and octanoic acid were seen as the initial products. However, on continued incubation, the octanal concentration progressively decreased to where only negligible quantities were present in the incubation after 10 min. The production of NADH was biphasic. An initial phase was followed in about 2 min with a slo...
The use of steady-state treatment in the rapid kinetics of horse liver alcohol dehydrogenase. The evaluation of data on the amplitude of the “burst” reaction.
Archives of biochemistry and biophysics    January 1, 1975   Volume 166, Issue 1 16-24 doi: 10.1016/0003-9861(75)90359-8
Tatemoto K.No abstract available
A steady-state kinetic model of butyrylcholinesterase from horse plasma.
The Biochemical journal    September 1, 1974   Volume 141, Issue 3 825-834 doi: 10.1042/bj1410825
Augustinsson KB, Bartfai T, Mannervik B.The steady-state kinetics of the butyrylcholinesterase-catalysed hydrolysis of butyrylthiocholine and thiophenyl acetate were shown to deviate from Michaelis-Menten kinetics. The ;best' empirical rate law was selected by fitting different rate equations to the experimental data by non-linear regression methods. The results were analysed in view of two alternative interpretations: (1) the reaction is catalysed by a mixture of enzymes, or (2) the activity is due to a single enzyme displaying deviations from Michaelis-Menten kinetics. It was concluded that the second alternative applies, and this...
Aromatic phosphoryl thiocholines. 3. The kinetics of inhibition of purified horse serum cholinesterase.
Arhiv za higijenu rada i toksikologiju    February 1, 1973   Volume 24, Issue 2 117-126 
Maksimović M, Cosić M, Binenfeld Z.No abstract available
Mechanistic studies on horse liver alcohol dehydrogenase. The influence of the different premixings on the transient kinetics of aldehyde reductions.
Biochemistry    June 6, 1972   Volume 11, Issue 12 2303-2310 doi: 10.1021/bi00762a015
Luisi PL, Favilla R.No abstract available