Lactate dehydrogenase quantification and isoenzyme distribution in physiological response to stress in red deer (Cervus elaphus).

As a contribution to the description of the physiological response to stress in red deer (Cervus elaphus), the potential use of the intracellular glycolytic enzyme, lactate dehydrogenase (LDH) and its isoenzyme LDH-5, as a marker of muscle damage was assessed. The distribution of LDH isoenzymes within red deer tissues was similar to that shown in other ruminants: tissue characterisation showed isoenzyme LDH-5 to be particularly associated with skeletal muscle. High plasma concentrations of creatine kinase, a muscle-specific enzyme, were associated with both high total LDH activity and the percentage of LDH-5 activity in deer undergoing a potentially stressful procedure, transportation followed by simulated abattoir lairage, which is further evidence of the specificity of the isoenzyme for skeletal muscle damage. The activity of LDH was not correlated with the plasma concentration of cortisol, a widely used physiological measure of psychological stress. This may have been due to different time courses for release and the fact that, in the present study, the immediate pre-collection procedures may have induced a short-term stress response.

Evaluation of serum iso-amylase in the normal dog using an improved electrophoretic technique.

Six iso-amylase fractions are known to exist in human serum, three originating from the salivary glands and three from the pancreas. Although it is known that a different number and source of iso-amylase fractions occur in the dog, the routine detection of all the canine iso-amylase fractions has not been previously established. Earlier methods detected either two iso-amylase fractions or, in a proportion of cases, four fractions. A method is described which detects four iso-amylase fractions in 95% of normal canine serum samples. Trials have shown the method is reproducible and that freezing at -40 degrees C has no effect on iso-amylase activity. The normal values for iso-amylase are recorded in 18 normal dogs.

A study of the interaction between bromocresol green dye and bovine, ovine and equine serum globulins.

In human medicine it has been shown that the bromocresol green (BCG) dye-binding method for the determination of serum albumin is not entirely specific, the dye reacting also with certain human serum globulins. This causes over-estimation of albumin when reaction times are prolonged beyond 30 seconds. In the present study, serum albumin values obtained from three animal species by the "immediate", i.e. less than 30 seconds, BCG reaction were compared with those by the 10-minute BCG reaction. Albumin-depleted sera were prepared using an affinity chromatography technique and their reactions and those of purified gamma globulin preparations with the dye were studied. In cattle, sheep and horses, serum albumin values obtained by the 10-minute reaction were higher than those obtained by the "immediate" BCG reaction, the differences being statistically significant. Purified gamma globulin did not react with the BCG dye after 10 minutes, but other globulins did. There were differences between the species in the magnitude of the reaction of their globulins with BCG dye.

Serum albumin values from healthy cattle, sheep and horses determined by the immediate bromocresol green reaction and by agarose gel electrophoresis.

Serum albumin concentrations were measured by the immediate reacting bromocresol green (BCG) method and by agarose gel electrophoresis in healthy cattle, sheep and horses. No statistically significant differences were found between the values obtained by the two methods. The immediate reacting BCG method is quicker and cheaper when used under the conditions described.

Serum protein values from clinically normal cats and dogs determined by agarose gel electrophoresis.

Serum protein electrophoretic values are presented from clinically normal cats and dogs. The Rf values (relative mobilities), relative (per cent) and absolute (g per litre) values for each protein fraction identified are given as means (mean) +/- s (one standard deviation). Electrophoretic Rf values produced by other authors using the same technique are very similar to those presented in this study but several of their relative and absolute values are at variance, as are total protein values using a comparable technique. These values were, however, obtained from animals resident in North America and were probably derived from populations of different breed composition to those used in this work. The environmental and dietary conditions to which these animals were normally subjected were also likely to have been different from those kept in the United Kingdom.

Species characteristics of serum proteins demonstrated after agarose gel electrophoresis.

Serum samples from five species of domestic animals were subjected to protein electrophoresis on commercially prepared agarose gel films. After processing, the strained electrophoretic patterns and densitometric traces exhibited certain characteristics for each species. The features which were considered distinctive of each species are illustrated.

A comparison of the serum protein electrophoretic patterns of young and adult animals.

Samples of serum from both young and adult normal cattle, sheep and horses were subjected to protein electrophoresis on agarose gel films. After processing, the stained electrophoretic patterns and densitometric traces of each species exhibited certain specific characteristics. The separations also revealed differences between young and adult animals of the same species. These age-related differences are described here.