Maintaining mineral homeostasis as well as the secretion and metabolism of mineralotropic hormones is important for healthy of periparturient dairy cows. To increase the activity of mineralotropic hormones, blood pH can be adjusted. The purpose of this study was to investigate changes in blood pH and the mechanism of action of this change in induced hypercalcaemic cows. Six non-lactating Holstein cows were used in a 2 × 2 crossover design. To induce hypercalcaemia, calcium borogluconate was administered subcutaneously to experimental cows and normal saline was administered subcutaneously to control cows. Blood and urine samples were collected serially after administration. Whole blood without any anticoagulant was processed with a portable blood gas analyser. Plasma concentration and urinary excretion of calcium were measured. In hypercalcaemic cows, both blood and urine calcium levels were significantly increased at 8 h compared to those at 0 h (P < 0.05), and a spontaneous increase in blood pH was also observed. The calcium concentration in plasma was highest at 2 h after administration (3.02 ± 0.27 mmol/L). The change in pH correlated with that in bicarbonate (r = 0.781, P < 0.001) rather than that in partial pressure of CO₂ (r = 0.085, P = 0.424). Hypercalcaemia induced a spontaneous change in blood pH through the bicarbonate buffer system and this system may be a maintainer of calcium homeostasis.

Due to the widespread occurrence of acrylamide in the environment, its likely carcinogen status, and the suitability of the pig model as a human analogue, the authors decided to evaluate the impact of high and low doses of this compound on the processes of erythropoiesis in swine bone marrow. The experiment was carried out on Danish Landrace pigs at the age of eight weeks and body weight about 20 kg. The animals were divided into three equal groups consisting of five pigs in each. Control animals received empty gelatin capsules (placebos). Animals from the first experimental group received a low dose of acrylamide of 0.5 μg/kg b.w./day (> 99% purity; Sigma-Aldrich, Poland), and animals from the second experimental group received a dose 10 times higher. Placebos and acrylamide capsules were administered with feed every morning for 28 days. After anaesthetisation of the animals, bone marrow from the femur was collected into tubes without an anticoagulant on days 0 and 28. After drying and staining, bone marrow smears were subjected to detailed cytological evaluation using a light microscope. This study showed that high and low doses of acrylamide affected the process of porcine erythropoiesis. The cytotoxic effect of acrylamide on this process was demonstrated in a change of the polychromatic erythroblasts/normochromatic erythroblasts ratio. Both doses of acrylamide caused a decrease in the number of ortho- and polychromatic erythroblasts.

Due to the widely documented and diverse toxic effects of acrylamide, the authors decided to evaluate the impact of high and low doses of this compound on the process of granulopoiesis in porcine bone marrow. The experiment was conducted on 15 Danish Landrace pigs at the age of 8 weeks. The animals were randomly assigned into three equal groups (n = 5). Control animals received empty gelatine capsules as placebo. Animals in the first experimental group (the LD group) received a low dose of acrylamide of 0.5 μg/kg b.w./day, and animals in the second experimental group (the HD group) received a tenfold higher dose of acrylamide of 5 μg/kg b.w./day. Placebo and acrylamide capsules were administered with feed every morning for 28 days. Bone marrow was collected into tubes without an anticoagulant twice – before the first capsule administration (day 0) and on the 28ᵗʰ day of the study. After drying and staining, bone marrow smears were subjected to detailed cytological evaluation under a light microscope. Changes in cell morphology, i.e. degenerative changes in the cellular nuclei, were observed in both experimental groups. Both low and high doses of acrylamide decreased the number of segmented eosinophils, neutrophilic and segmented metamyelocytes, neutrophils, as well as basophils and basophilic metamyelocytes. Acrylamide at doses of 0.5 μg/kg b.w./day and 5 μg/kg b.w./day clearly influences porcine granulopoiesis.

OBJECTIVE To compare blood glucose concentrations of black-tailed prairie dogs (Cynomys ludovicianus) measured by use of a variety of portable analyzers with results from a laboratory biochemistry analyzer. SAMPLE Venous blood samples (3 mL) obtained from each of 16 healthy black-tailed prairie dogs. PROCEDURES A portion of each blood sample was used to measure glucose concentrations by use of an amperometric human point-of-care glucometer and a colorimetric species-specific portable blood glucose meter designed for veterinary use with both canine (code 5) and feline (code 7) settings. The remainder of each blood sample was placed into 2 tubes (one contained lithium heparin and the other contained no anticoagulant). A portable veterinary chemistry analyzer (PVCA) and a handheld analyzer were used to measure glucose concentration in heparinized blood. Serum glucose concentration was measured in the remaining portion by use of a biochemistry analyzer. A general linear mixed models approach was used to compare glucose concentrations and measurement bias obtained with the various measurement methods. RESULTS Measurement bias and differences in mean glucose concentrations were apparent with all measurement methods. In particular, the veterinary glucometer, whether used on the canine or feline setting, overestimated mean glucose concentrations, whereas the human glucometer, PVCA, and handheld analyzer underestimated mean glucose concentrations relative to the concentration obtained with the biochemistry analyzer. CONCLUSIONS AND CLINICAL RELEVANCE Results indicated that none of the measurement methods provided consistently accurate blood glucose concentrations of black-tailed prairie dogs, compared with values determined with a biochemistry analyzer.

The commercial snake venom extract, Protac, is a specific activator of the anticoagulant zymogen, protein C (PC) in human plasma. This specific action has led to its use in developing coagulation-based and amidolytic-based assays for the diagnosis of quantitative and/or qualitative PC deficiency states in human beings. The purpose of the present study was to compare the effects of Protac on the activated partial thromboplastin times (APTT) of human, bovine, equine, and canine plasmas in order to determine the potential value of this venom extract as an activator in functional PC assays in these domestic animal species. As expected, Protac significantly prolonged the APTT of normal human plasma, but had no effect on plasma known to be devoid of PC. Clotting times were prolonged by 34%-214% with concentrations of venom activator ranging from 0.1-1.0 U/mL. Under identical conditions, Protac prolonged the APTT of equine plasma by 11%-98% over control times. Even more dramatic was the inhibitory effect of Protac on the clotting of bovine plasma, extending the APTT more than 3-fold at a venom concentration of 0.1 U/mL. At higher venom concentrations, most bovine plasmas remained unclotted after 300 s (control time 34.1 s). Under similar conditions, the canine APTT was unaffected by Protac, even when the venom concentration was increased to 3 U/mL. In order to determine the reason for the lack in response of canine plasma, the concentration of the APTT reagent was altered (decreased), exposure time of the plasma to the Protac was increased from 2 min to 9 min, and the plasma was diluted to assess for the potential existence of plasma PC inhibitors. Protac caused an unexpected shortening of the APTT when the contact activator reagent was diluted. Increasing the exposure time had no effect. Although a slight prolongation of the canine APTT was detected when the plasma was diluted, the presence of strong plasma PC inhibition was considered an unlikely cause of the lack of significant anticoagulant action. The failure of Protac to exert a strong inhibitory effect on the canine APTT, as well as to generate amidolytic activity, suggests that this venom extract does not stimulate the production of activated PC activity in canine plasma. This may result from molecular differences in the canine PC molecule that prevent the formation of the stoichiometric complex of venom extract, APTT reagent, and canine protein, a complex thought to be essential for the PC-activating function of Protac. Protac may be suitable as an activator of PC in bovine and equine plasmas; however, it appears ineffective in generating anticoagulant activity in canine plasma.

Thirty healthy male horses were allotted to 3 groups and treated blindly during 4 days. Group-1 horses received unfractioned calcium heparin (100 IU/kg of body weight, SC, q 12 h). Group-2 horses received a single dose of a low-molecular-weight heparin (50 anti-Xa IU/kg, SC) every morning, and a similar volume of saline solution every evening. Group-3 horses received the vehicle (saline solution), SC, every 12 hours. Citrated and EDTA-anticoagulated blood samples were collected before starting the medication (T-0) and once daily 3 hours after each morning injection (T-3, T-27, T-51, and T-75). The PCV, hemoglobin concentration, RBC and platelet counts, and clotting times (activated partial thromboplastin time and thrombin time) were determined, and a microscopic examination to detect hemagglutination was performed. Plasma concentration of heparin was measured by use of the antifactor Xa activity assay. Bleeding time was determined on the first and fourth days, using a double-template method. The horses given unfractioned heparin had marked agglutination of erythrocytes after the first injection that became more pronounced as treatment progressed. Also, significant decrease in PCV, hemoglobin concentration, and RBC count was observed during treatment. Platelet count was significantly decreased after the first day, and clotting times were significantly prolonged. In contrast to the horses given unfractioned heparin, those given low-molecular-weight heparin did not have any agglutination of erythrocytes during the 4 days of treatment, and there were no significant changes in PCV, hemoglobin concentration, or RBC and platelet counts. Activated partial thromboplastin time increased slightly in the horses given low-molecular-weight heparin, although the values remained within reference range. Both groups of horses achieved adequate concentrations of heparin in plasma for prophylactic purposes, but those given low-molecular-weight heparin achieved those values after the first injection. Bleeding times were not significantly different between heparin-treated horses and horses given saline solution during treatment. We conclude that low-molecular-weight heparin may be used more safely and conveniently in horses, because it does not affect equine erythrocytes, platelets, or clotting and bleeding times.

A solid-phase ELISA to detect antibodies bound to the surface of canine platelets (platelet-bound antibodies) is described. Using this assay, the effect of anticoagulant and storage time of anticoagulant blood on the concentration of antibodies bound to the surface of platelets from clinically normal dogs was investigated. Blood from 3 clinically normal dogs was anticoagulated with acid citrate dextrose, Na3 citrate, and aqueous K3 EDTA and stored on ice for up to 48 hours. Platelet-bound antibody concentration was measured on platelets isolated from anticoagulated blood immediately after venipuncture and subsequent to storage of blood for 24 and 48 hours. Differences in platelet-bound antibody concentrations were investigated among dogs, anticoagulants, and storage times by ANOVA and Bonferroni pair-wise comparison of means. There was no effect of dog on platelet-bound antibody concentration. The effect of time was significant (P < 0.0001), with higher concentration of platelet-bound antibodies detected with increasing storage time. Effect of anticoagulant on platelet-bound antibody concentration was not statistically significant; however, there was a trend to increasing concentration of antibodies bound to platelets isolated from Na3 citrate- and K3 EDTA-anticoagulated blood. Moreover, there was significant (P = 0.02) interaction between anticoagulant and time. Platelet-bound antibody concentration increased with storage of anticoagulated blood prior to platelet isolation and with use of Na3 citrate and K3 EDTA anticoagulants. The preferred anticoagulant for platelet-bound antibody measurement is acid citrate dextrose. Platelet-bound antibody concentration should be determined not longer than 24 hours after blood collection.

We evaluated the effect of anticoagulant (lithium heparin, sodium heparin, or none) and type of autoanalyzer on selected blood biochemical values of the loggerhead sea turtle (Caretta caretta). More differences were observed between the analytes in serum and those in the 2 types of plasma than were observed between the 2 types of plasma. Differences in electrolyte concentrations were not significant when plasma from sodium-heparinized blood was compared with plasma from lithium-heparinized blood. Serum is not recommended for reptilian studies because clot formation is unpredictable and because the time required for clotting may allow substantial changes in the chemical composition of the sample. For most determinants, values varied more between the 2 types of autoanalyzers than among the 3 anticoagulant treatments. These sources of variation must be considered when performing comparative studies.

Swine plasminogen is not activated by staphylokinase of Staphylococcus aureus. In this study, the activation of swine plasminogen by staphylokinase of Staph hyicus subsp. hyicus was investigated and the effect of EDTA(disodium) on plasminogen activation was also studied. When the activation of swine plasminogen by staphylokinase of Staph hyicus subsp. hyicus was examined in fresh swine plasma, swine plasminogen could be weakly activated. However, when EDTA was added to the swine plasma, plasminogen activation was markedly enhanced, but this enhancement was not observed on bovine fibrin-dog plasminogen agar plate containing EDTA. Chicken and bovine plasminogens were not activated by staphylokinase of Staph hyicus subsp. hyicus. Using fresh swine plasma agar containing 0.07% EDTA, staphylokinase activity was detected in 96.3% of Staph hyicus subsp. hyicus strains isolated from pigs and in none of the chicken and bovine strains.