Analyze Diet

Topic:Protein

Proteins are essential macromolecules that play diverse roles in the physiology and health of horses. They are composed of amino acids and are involved in various biological processes, including tissue growth, repair, and the synthesis of enzymes and hormones. Dietary proteins are a key component of equine nutrition, influencing muscle development, immune function, and overall performance. Horses require a balanced intake of essential amino acids, which must be obtained through their diet, as they cannot be synthesized endogenously. This page compiles peer-reviewed research studies and scholarly articles that explore the types, functions, and dietary requirements of proteins in horses, as well as their impact on equine health and performance.
Equine anti-hapten antibody. IV. The effect of polyalanylation on affinity.
Immunochemistry    July 1, 1967   Volume 4, Issue 4 259-267 doi: 10.1016/0019-2791(67)90187-5
Karush F, Sela M.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
Purification and crystallization of horse prothrombin.
Biochemical and biophysical research communications    May 25, 1967   Volume 27, Issue 4 505-510 doi: 10.1016/s0006-291x(67)80015-9
Miller KD, Phelan AW.No abstract available
[Preliminary observations on the serum proteins of the horse, donkey and their interspecific hybrids. I. Preliminary investigations].
La Ricerca scientifica    April 1, 1967   Volume 37, Issue 4 376-378 
Bonadonna T, Fornaroli D, Succi G.No abstract available
[Tissue antigens of the digestive tract in man and animals. II. Antigens of the colon].
Pathologie et biologie    April 1, 1967   Volume 15, Issue 7 359-367 
Zweibaum A, Halpern B, Veyre C, Oriol-Palou R.No abstract available
The electrophoretic pattern of serum proteins in normal animals.
Research in veterinary science    April 1, 1967   Volume 8, Issue 2 137-142 
Irfan M.The normal electrophoretic pattern and values for total and differential serum proteins have been determined for 100 cattle, 70 horses, 15 dogs, and 24 rabbits. Comparative studies were also made on 10 pigs, 10 goats, 10 sheep and 15 domestic fowls. The mean total serum protein for normal cattle was 7·16 g.%. The individual protein fractions were: albumen 43·1; alpha-globulin 110; beta-globulin 12·0; gamma-globulin 33·9%. The mean total serum protein for normal horses was 7·3 g.%. The individual protein fractions were: albumen 33·5; globulins: alpha-1 15·0, alpha-2 16·0, beta-globul...
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
Equine antihapten antibody. The subunits and fragments of anti-beta-lactoside antibody.
The Journal of experimental medicine    February 1, 1967   Volume 125, Issue 2 249-275 doi: 10.1084/jem.125.2.249
Rockey JH.Eight antigenically unique immunoglobulins have been identified in purified equine anti-p-azophenyl-beta-lactoside (Lac) antibody isolated from a single horse. The Fc fragments of the gammaGa-, gammaGb-, gammaGc-, and -gammaA-globulins have been shown to possess unique antigenic determinants. Common gammaG- and gammaA-Fc fragment antigenic determinants, which were absent from the 10Sgamma(1)- and gammaM-globulins, have also been observed. All antibody populations share two antigenically distinct light (B, L) chain variants. The association of anti-Lac antibody with the hapten p-(p-dimethylamin...
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
Release of human and horse fibrinopeptides.
Acta chemica Scandinavica    January 1, 1967   Volume 21, Issue 7 1879-1886 doi: 10.3891/acta.chem.scand.21-1879
Teger-Nilsson AC.No abstract available
Variation of horse prealbumins in acidic starch gels.
Acta veterinaria Scandinavica    January 1, 1967   Volume 8, Issue 2 193-194 doi: 10.1186/BF03547846
Braend M.Working with acidic starch gels (pH 5.9) (1965) detected a large number of horse serum protein zones migrating faster than the albumins. In the present communication these proteins shall be called acidic prealbumins or just prealbumins.
[Heterogeneity of horse spleen ferritin. I. Comparison of “free” apoferritin and alfa-ferritin].
Seikagaku. The Journal of Japanese Biochemical Society    January 1, 1967   Volume 39, Issue 1 23-28 
Shinjyo S, Kume M, Danjo T.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
Erythrocyte sedimentation rate and protein-bound carbohydrates in domestic animals.
Acta veterinaria Scandinavica    January 1, 1967   Volume 8, Issue 3 279-286 doi: 10.1186/BF03547833
Böttiger LE.Erythrocyte sedimentation rate, total protein and fibrinogen, electrophoretic protein pattern, and total serum protein-bound carbohydrates have been determined in a number of domestic animals and compared to human values. The striking finding is that although the E.S.R. varies widely between various species, the fibrinogen content is of the same order of magnitude in all. The horse, which shows a very high E.S.R., has a well marked beta-globulin fraction as an outstanding feature, a finding that should be further studied. Blutsenkungsgeschwindigkeit, Gesamteiweiss und Fibrinogen, elektroforeti...
Structure of the immunogobulins.
Giornale di malattie infettive e parassitarie    December 1, 1966   Volume 18, Issue 12 939-941 
Press EM.No abstract available
Comparison of the C-terminal amino-acid sequence of two horse immunoglobulins IgG and IgG(T).
Nature    October 8, 1966   Volume 212, Issue 5058 205-206 doi: 10.1038/212205a0
Weir RC, Porter RR, Givol D.No abstract available
Studies on the proteins from chromaffin granules of ox, horse and pig.
Nature    August 27, 1966   Volume 211, Issue 5052 982-983 doi: 10.1038/211982a0
Winkler H, Ziegler E, Strieder N.No abstract available
Comparison of the structure of the immunoglobulins from horse serum.
The Biochemical journal    July 1, 1966   Volume 100, Issue 1 63-68 doi: 10.1042/bj1000063
Weir RC, Porter RR.A study of the chemical structure of the horse immunoglobulins IgG and IgA(T) has shown that the amino acid contents of the peptide chains are very similar. These globulins differ most markedly in the products of papain digestion. IgG gives 3.5s products, whereas IgA(T) gives a 5s fraction and smaller components. This difference appears to be associated with the presence of an additional easily reducible disulphide bond in the Fd fragment of the heavy chain. There is two to three times as much carbohydrate in IgA(T) as in IgG. In both, this is in the heavy chain and in IgA(T) more than half is...
Comparative studies on the soluble protein fractions of bovine, equine, porcine and ovine adrenal chromaffin granules.
The Biochemical journal    July 1, 1966   Volume 100, Issue 1 6C-7C doi: 10.1042/bj1000006c
Helle KB.No abstract available.
Changes in horse serum proteins & antibody proteins after hyperimmunization & repeated bleedings.
Indian journal of biochemistry    June 1, 1966   Volume 3, Issue 2 128-130 
Acharya US, Buduk DP, Rao SS.No abstract available
[Studies on tissue culture of equine infectious anemia virus. VII. Evaluation of bovine serum used for equine leukocyte culture with special reference to the relationship between the serum protein fraction pattern and the culture growth].
Nihon juigaku zasshi. The Japanese journal of veterinary science    June 1, 1966   Volume 28, Issue 3 119-128 doi: 10.1292/jvms1939.28.119
Watanabe S.No abstract available
Compartmentalization and turnover of 131-I-labeled albumin and gamma globulin in horses.
American journal of veterinary research    May 1, 1966   Volume 27, Issue 118 699-705 
Matteeuws DR, Kaneko JJ, Loy RG, Cornelius CE, Wheat JD.No abstract available
Electrophoretic behavior of mammalian-type cytochromes c.
The Journal of biological chemistry    April 10, 1966   Volume 241, Issue 7 1473-1477 
Barlow GH, Margoliash E.No abstract available
Studies on the inheritance of electrophoretic forms of transferrins, albumins, prealbumins and plasma esterases of horses.
Genetics    April 1, 1966   Volume 53, Issue 4 681-694 doi: 10.1093/genetics/53.4.681
Gahne B.No abstract available
[Purification of horse antipoliomyelitic antibodies]. Calothy G, Digeon M, Raynaud M.No abstract available
Appearance of pre-alpha-2-globulins soon after the very first dose of diphtheria toxoid in horse.
Experientia    March 15, 1966   Volume 22, Issue 3 167-168 doi: 10.1007/BF01897714
Acharya US, Rao SS.No abstract available
N-terminal sequence of horse spleen apoferritin.
Archives of biochemistry and biophysics    January 1, 1966   Volume 113, Issue 1 1-4 doi: 10.1016/0003-9861(66)90149-4
Suran AA.No abstract available
[Study of some oligopeptides isolated from chymotrypsin hydrolysates of horse myoglobin globin].
Bulletin de la Societe de chimie biologique    January 1, 1966   Volume 48, Issue 5 733-735 
Boulanger Y, Dautrevaux M, Han KK, Biserte G.No abstract available
[Study of the “median” peptide freed from horse myoglobin by cyanogen bromide].
Bulletin de la Societe de chimie biologique    January 1, 1966   Volume 48, Issue 8 995-997 
Han K, Dautrevaux M, Boulanger Y, Biserte G.No abstract available