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        Lablab purpureus SEED AS A SUPPLEMENT FOR GOATS FED LOW QUALITY ROUGHAGE

        Ismartoyo, I.,Dixon, R.M.,Slocombe, R.F.,Holmes, J.H.G. Asian Australasian Association of Animal Productio 1993 Animal Bioscience Vol.6 No.4

        Young goats were fed low quality roughage ad libitum and supplements of insect-damaged Lablab purpureus (var. Highworth) seed fed at approximately 3, 6 or 12 g/kg liveweight (LW), or sweet lupin seed (Lupinus angustifolius var. Uniharvest) fed at 12 g/kg LW. Roughage intake was not changed by 3 or 6 g/kg LW levels of Lablab or by 12 g/kg LW lupin supplement, but was reduced (p<0.05) by 35% by 12 g/kg LW Lablab supplement. Organic matter (OM) digestibility was increased by all supplements, and digestible OM intake was increased by the 6 g/kg LW Lablab and 12 g/kg LW lupin supplements. LW gain and feed conversion ratio were not changed by 3 or 6 g/kg LW Lablab or the 12 g/kg LW lupin, but were reduced (p<0.05) by 12 g/kg LW Lablab supplement. It was concluded that young goats could efficiently utilize supplements of Lablab purpureus seed fed at levels of up to 6 g/kg LW. However, when 12 g/kg of the Lablab seed was fed, poor performance suggested that the goats were adversely affected by anti-nutritional factors which were not neutralized by rumen fermentation.

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        Determination of angiotensin I-converting enzyme activity in equine blood: lack of agreement between methods of analysis

        Maria Fernanda de M. Costa,Adriana K. Carmona,Marcio F. M. Alves,Timothy M. Ryan,Helen M. Davies,Garry A. Anderson,Ron F. Slocombe 대한수의학회 2011 Journal of Veterinary Science Vol.12 No.1

        Angiotensin-I converting enzyme (ACE) is a key regulator of blood pressure, electrolytes and fluid homeostasis through conversion of angiotensin I into angiotensin II. Recently, a genetic polymorphism of the ACE gene, which accounts for 47% of the variation of ACE activity in blood, has been advocated as a biomarker of athletic aptitude. Different methods of analysis and determination of ACE activity in plasma have been used in human and equine research without a consensus of a “gold standard” method. Different methods have often been used interchangeably or cited as being comparable in the existing literature; however, the actual agreement between assays has not been investigated. Therefore, in this study, we evaluated the level of agreement between three different assays using equine plasma obtained from 29 horses. Two spectrophotometric assays using Furylacryloylphenylalanyl-glycyl-glycine as substrate and one fluorimetric assay utilizing o-aminobenzoic acid-FRK-(Dnp)P-OH were employed. The results revealed that the measurements from the different assays were not in agreement, indicating that the methods should not be used interchangeably for measurement of equine ACE activity. Rather, a single method of analysis should be adopted to achieve comparable results and critical appraisal of the literature is needed when attempting to compare results obtained from different assays.

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