Topic:Biochemistry

The study of biochemistry in horses encompasses the chemical processes and substances that occur within equine organisms. This field investigates the molecular interactions and pathways that are fundamental to horse physiology, including metabolism, enzyme activity, and genetic expression. Key areas of interest include the examination of metabolic disorders, nutrient absorption, and the biochemical basis of muscle function and energy production. Researchers utilize biochemical analysis to understand health and disease mechanisms in horses, contributing to the development of diagnostic tools and therapeutic strategies. This page gathers peer-reviewed studies and scholarly articles that explore various biochemical processes and their implications for equine health and performance.

Characterization of the forssman glycolipid hapten of horse kidney by mass spectrometry.

The Journal of biological chemistry August 10, 1974 Volume 249, Issue 15 4819-4823

Karlsson KA, Leffler H, Samuelsson BE.No abstract available

Zentralblatt fur Veterinarmedizin. Reihe A August 1, 1974 Volume 21, Issue 8 638-643 doi: 10.1111/j.1439-0442.1974.tb01348.x

Muylle E, Oyaert W, De Roose P, Van Den Hende C.No abstract available

Archives of biochemistry and biophysics August 1, 1974 Volume 163, Issue 2 581-588 doi: 10.1016/0003-9861(74)90517-7

Hunter SJ, Fletcher MA, Bush CA.No abstract available

Journal of the American Veterinary Medical Association August 1, 1974 Volume 165, Issue 3 262-264

Carlson GP, Mansmann RA.No abstract available

Endocrinology August 1, 1974 Volume 95, Issue 2 417-420 doi: 10.1210/endo-95-2-417

Sato T, Iesaka T, Jyujo T, Taya K, Ishikawa J.No abstract available

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Horse pancreatic ribonuclease.

European journal of biochemistry July 15, 1974 Volume 46, Issue 2 221-233 doi: 10.1111/j.1432-1033.1974.tb03615.x

Scheffer AJ, Beintema JJ.No abstract available

Comparative biochemistry and physiology. B, Comparative biochemistry July 15, 1974 Volume 48, Issue 3 427-433 doi: 10.1016/0305-0491(74)90277-6

Zech R, Zürcher K.No abstract available

European journal of biochemistry July 15, 1974 Volume 46, Issue 2 387-391 doi: 10.1111/j.1432-1033.1974.tb03631.x

Margalit R, Schejter A.The specific binding of cations to horse heart ferrocytochrome c has been studied, using the gel filtration method. The cations investigated were: Mg2+, Co2+, cinchonine and proflavine. The stability constants are in the range of 5-8 mM-1, and the number of binding sites per protein molecule are 1 to 2. The temperature dependence of the stability constant for the Mg2+-ferrocytochrome system was measured. The thermodynamic parameters were found to be: dH&s = 4-12 kcal/mol, dG;,, (25 "C) = -5.6 kcal/mol and AS&, = +57 calxmol-lx K-I.

Research in veterinary science July 1, 1974 Volume 17, Issue 1 42-48

Roberts MC, Hill FW, Kidder DE.No abstract available

American journal of veterinary research July 1, 1974 Volume 35, Issue 7 997-1001

Oxender WD, Noden PA, Louis TM, Hafs HD.No abstract available

Mikrobiolohichnyi zhurnal July 1, 1974 Volume 36, Issue 4 516-518

Narepekha OM.No abstract available

Proceedings of the National Academy of Sciences of the United States of America July 1, 1974 Volume 71, Issue 7 2892-2894 doi: 10.1073/pnas.71.7.2892

Wilgus H, Stellwagen E.Changes in the visible absorbance spectra of complexes of horse heart cytochrome c hemopeptide 1-65, peptide 66-104, and their guanidinated counterparts are compared with those characteristic of native and fully guanidinated ferricytochrome c over the pH range 7 to 11. Upon raising the pH, the methionine ligand in the guanidinated hemopeptide 1-65.peptide 66-104 complex is replaced by a strong field ligand. By contrast, the methionine ligand in the hemopeptide 1-65.guanidinated peptide 66-104 is replaced by a weak field ligand. These results demonstrate that lysine 13 does not ligate with the ...

Infection and immunity July 1, 1974 Volume 10, Issue 1 116-122 doi: 10.1128/iai.10.1.116-122.1974

Woolcock JB.A cell wall component of Streptococcus equi analogous to the M protein of group A streptococci has been identified and purified. A highly purified product has been obtained from cells by hot acid extraction, followed by acid precipitation, ammonium sulfate fractionation, and column chromatography. This product reacts with S. equi antiserum. The existence of this fraction in S. equi has been confirmed by the failure of trypsin-treated cells and their extracts to remove the long-chaining capacity of S. equi antiserum. The antigenicity of this M-like protein when incorporated in adjuvant has been...