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Author Koenen, E.P.C.; Aldridge, L.I.; Philipsson, J. url  openurl
  Title An overview of breeding objectives for warmblood sport horses Type Journal Article
  Year 2004 Publication Livestock Production Science Abbreviated Journal  
  Volume 88 Issue 1-2 Pages 77-84  
  Keywords Breeding objective; Sport horse; Sport performance; Conformation; Specialisation  
  Abstract The aim of this paper is to review the current breeding objectives of organisations that run a selection programme for warmblood riding horses in the light of an increasing trend in trade of semen across countries. In a questionnaire, 19 horse breeding organisations provided information on breeding objective traits. Variation both in length and amount of details used to define individual breeding objectives was large, reflecting that many traits in sport horse breeding are not easy to measure, and therefore, have to be defined in a subjective way. The majority of the breeding objectives included conformation, gaits and performance in show jumping and dressage. Some breeding objectives also included behaviour, soundness, health and fertility. However, several organisations did not specify the sport discipline and the level of competition (amateur, national or international level) in the breeding objective. In general, relative weightings of the traits within the verbally presented breeding objectives were not given, but were assessed by the organisations in response to this study. The relevance of more information on expected future production circumstances and on the genetic parameters of the traits of interest are discussed. A further review of the consistency, completeness and the number of traits of the present breeding objectives for sport horses is recommended to optimise the efficiency of selection decisions.  
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  Call Number refbase @ user @ Serial 3954  
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Author Koenen, E.P.C.; van Veldhuizen, A.E.; Brascamp, E.W. url  openurl
  Title Genetic parameters of linear scored conformation traits and their relation to dressage and show-jumping performance in the Dutch Warmblood Riding Horse population Type Journal Article
  Year 1995 Publication Livestock Production Science Abbreviated Journal  
  Volume 43 Issue 1 Pages 85-94  
  Keywords Horse; Heritability; Conformation; Dressage; Show jumping  
  Abstract In this study genetic parameters of linear scored conformation traits of the Dutch Warmblood Riding Horse were estimated in relation to performance in competition. Observations on 10 665 mares were analyzed with an animal model including the fixed effects age, classifier, location and percentage of thoroughbred. Using restricted maximum likelihood algorithms, heritabilities of 26 linear scored conformation traits were estimated in the range 0.09-0.28. Several conformation traits had high up to very high mutual genetic correlations. Competition results of 3476 horses with performance in dressage and 3220 horses with performance in show-jumping were linked to the conformation data to estimate the genetic relationship between conformation and performance in competition. The model for the evaluation of the competition results included the fixed effects riding club, age and sex. Estimated heritabilities for dressage and show-jumping were 0.17 +/- 0.05 and 0.19 +/- 0.04, respectively. Genetic correlations between conformation and performance were low to moderate. The length of the neck, length and position of the shoulders, shape and length of croup and muscularity of the haunches had a significant moderate genetic correlation with dressage. Muscularity of the neck, shape of the croup and muscularity of the haunches had a significant genetic correlation with show-jumping. The results indicate that, due to the low genetic correlations with performance traits, indirect selection for performance using conformation results is of limited value.  
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  Call Number refbase @ user @ Serial 3961  
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Author Cho, K.C.; Chan, K.K. url  openurl
  Title Kinetics of cold-induced denaturation of metmyoglobin Type Journal Article
  Year 1984 Publication Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology Abbreviated Journal  
  Volume 786 Issue 1-2 Pages 103-108  
  Keywords Metmyoglobin denaturation; Temperature jump; Denaturation kinetics; Conformational transformation; (Horse heart)  
  Abstract Using a slow temperature-jump spectrophotometer, we have studied the kinetics of cold-induced denaturation of metmyoglobin between 0[degree sign]C and 20[degree sign]C at acidic pH. The time-scale of the transition is slow and is of the order of minutes. The results are consistent with the transition's involving a total of three states, native (N), transient intermediate (I) and denatured (D), which are converted from one to the other in that order.  
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  Call Number refbase @ user @ Serial 3978  
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Author Hagen, S.J.; Eaton, W.A. doi  openurl
  Title Two-state expansion and collapse of a polypeptide Type Journal Article
  Year 2000 Publication Journal of Molecular Biology Abbreviated Journal J Mol Biol  
  Volume 301 Issue 4 Pages 1019-1027  
  Keywords Animals; Computer Simulation; Cytochrome c Group/*chemistry/*metabolism; Horses; Kinetics; Lasers; Models, Chemical; Peptides/*chemistry/*metabolism; Protein Conformation; Protein Denaturation; *Protein Folding; Spectrometry, Fluorescence; Temperature; Thermodynamics  
  Abstract The initial phase of folding for many proteins is presumed to be the collapse of the polypeptide chain from expanded to compact, but still denatured, conformations. Theory and simulations suggest that this collapse may be a two-state transition, characterized by barrier-crossing kinetics, while the collapse of homopolymers is continuous and multi-phasic. We have used a laser temperature-jump with fluorescence spectroscopy to measure the complete time-course of the collapse of denatured cytochrome c with nanosecond time resolution. We find the process to be exponential in time and thermally activated, with an apparent activation energy approximately 9 k(B)T (after correction for solvent viscosity). These results indicate that polypeptide collapse is kinetically a two-state transition. Because of the observed free energy barrier, the time scale of polypeptide collapse is dramatically slower than is predicted by Langevin models for homopolymer collapse.  
  Address Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Building 5, Bethesda, MD, 20892-0520, USA  
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  ISSN 0022-2836 ISBN Medium  
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  Notes PMID:10966803 Approved no  
  Call Number Equine Behaviour @ team @ Serial 3790  
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