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Effects of exercise on serum aminotransferase activity and pyridoxal phosphate saturation in Thoroughbred racehorses
Author(s) -
REJ R.,
RUDOFSKY U.,
MAGRO A.,
PRENDERGAST J.
Publication year - 1990
Publication title -
equine veterinary journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.82
H-Index - 87
eISSN - 2042-3306
pISSN - 0425-1644
DOI - 10.1111/j.2042-3306.1990.tb04248.x
Subject(s) - pyridoxal 5 phosphate , pyridoxal phosphate , medicine , horse , endocrinology , pyridoxal , phosphate , chemistry , biochemistry , biology , enzyme , cofactor , paleontology
Summary Aminotransferase activities were measured in the serum of two‐ to three‐year‐old Thoroughbred fillies and colts during a four week period of peak training for flat racing. Aspartate aminotransferase (AspAT, EC 2.6.1.1), mitochondrial aspartate aminotransferase (m‐AspAT) and alanine aminotransferase (AlaAT, EC 2.6.1.2) activities in serum were measured and the relative proportions of apoenzyme and holoenzyme were determined. The aminotransferase activities were increased only slightly immediately following exercise. This small and immediate post exercise increase in activity did not vary greatly over the period of peak training. Measured in the presence of exogenous pyridoxal 5’‐phosphate, mean enzyme activities (iu/litre at 30°C) before exercise were: AspAT, 291; m‐AspAT, 13; AlaAT, 18. After exercise they were: AspAT, 317; m‐AspAT, 16; AlaAT, 23. Nearly all of the AspAT activity was present in the holoenzyme form (94 per cent holoenzyme) indicating excellent vitamin B 6 status in these animals. Paradoxically, the AlaAT in serum from the same highly trained Thoroughbred horses was poorly saturated with pyridoxal phosphate, with nearly half of the AlaAT in most horses present in the inactive apoenzyme form (61 per cent that of holoenzyme). It is critical therefore, that exogenous pyridoxal phosphate be included in aminotransferase assays to determine the amounts of enzyme release into the peripheral circulation.