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Electronic nose with sensors is used in many industries and for various applications such as quality control, process monitoring, shelf life evaluation, origin or authenticity assessment. The aim of this work was to investigate the electronic nose with FID detectors applicability for characterization of steamed cheese and for the assessment of steamed cheese quality decay during storage. Samples of smoked and unsmoked steamed cheese varieties from 5 Slovak enterprises concerning different regions of Slovakia were analysed. Data from aroma profiles were processed by statistical technique PCA. Compounds like acetaldehyde, 1-propanal, propanoic acid, ethyl hexanoate, furfural, butan-2-one, isovaleric acid, 1-hexanol or α-pinene were determined as significant flavours in fresh steamed cheese samples. In the current study, no significant differences in aroma profiles between fresh and stored cheese samples were confirmed. Thus, differences in main odour substances composition of steamed cheese varieties, obtained from various producers in several geographic regions of Slovakia, were minor.

The aim of the present study was to evaluate the effect of different storage time and temperature conditions on the concentration of serum total proteins and their electrophoretic fractions in goats. Blood samples were collected from 12 female of Girgentana goats and the obtained serum was divided into 4 aliquots. The first aliquot was analyzed immediately after separation (T 0 ); the second was refrigerated at 4 °C and analyzed after 24 (T 1 ), 48 (T 2 ), and 72 (T 3 ) hours; the third was stored at −20 °C immediately after centrifugation and analyzed after 2 days (T 4 ); and the last aliquot was stored at −20 °C after 24 h refrigeration and analyzed after 1 week (T 5 ). The serum total proteins, serum protein electrophoretic fractions (albumin, α-, β1-, β2- and γ-globulins) and albumin/globulin ratio (A/G) values were determined. A significant effect of storage conditions on serum total proteins, albumin, α1-, β2- and γ-globulins values was found (P 1 and T 4 than T 0 . Albumin showed higher concentrations at T 1 , T 2 , T 3 , T 4 and T 5 in respect to the values measured at T 0 . The concentration of α1-globulins was significantly higher at T 4 than T0; the β2-globulins values were lower at T 3 and T 5 respect to T 0 , whereas the γ-globulins values were lower at T 5 than T 0. Together these results showed that temperature and time of serum storage are important pre-analytical factors which affect concentrations of serum total proteins and their electrophoretic fractions in electrophoretic analysis. The results of present study suggest that fresh serum samples or samples refrigerated for 24 h are recommended for electrophoretic analysis to obtain accurate data, which can help clinicians to differentiate between sick and healthy animals.

The objective of this study was to evaluate the influence of colostrum intake on the serum protein electrophoretic pattern in clinically healthy calves, lambs and kids during the first two weeks of life, as well as differences in the protein profile between these species of ruminants. The study included three groups of clinically healthy calves (n = 12), lambs (n = 10) and kids (n = 7). The first blood sampling was performed before the colostrum intake (day 0) and then at 1, 2, 7 and 14 days of age. Blood serum was analysed for the concentrations of total proteins, serum protein electrophoretic fractions and albumin/globulin ratio. Serum protein electrophoresis identified in calves 6 (albumin, α1-, α2-, β1-, β2-, and γ-globulins) and in lambs and kids 5 (albumin, α1-, α2-, β- and γ-globulins) distinct bands. Significant changes were observed in the analysed parameters during the evaluated period in all groups of ruminants. Except of the concentration of total proteins in precolostral serum signifi...

This study was aimed at the evaluation of changes in the concentrations of selected blood serum proteins in calves during the first three months of life, including precolostral, colostral, milk, transitional and solid feeding period. Nine clinically healthy calves were used in this study. The first blood sampling was performed before the colostrum intake (day 0) and then at 1, 2, 7, 14, 30, 60, and 90 days of age. Blood serum was analyzed for the concentrations of α1-fetoprotein, prealbumin, transferrin, and lactoferrin. The results showed significant changes in the serum concentrations of all the evaluated proteins in calves during the first three months of life (P < 0.01 and P < 0.001). At birth, the mean concentration of α1-fetoprotein was low and increased more than × 8 at one day after colostrum intake, then a gradual decrease was found up to day 30 of life. Similar tendency was observed in the concentrations of prealbumin and lactoferrin. While the concentrations of prealbumin increased approximately × 3.5 at one day after colostrum intake, the serum lactoferrin values showed approximately 1.5-fold increase. A subsequent gradual decrease from the 2nd day of life was found for both prealbumin and lactoferrin. In the concentrations of transferrin, a significant increase was observed on day 7 (P < 0.05). The highest values were found at the age of 14 and 30 days. These results suggest that concentrations of these proteins in calves are markedly altered during the postnatal period, which should be taken into consideration for their precise interpretation in young animals.

The objective of this study was to describe the physiological changes in the concentrations of acute phase proteins (APPs) in calves during the first month of life, including pre-, postcolostral and milk feeding period. Seven clinically healthy calves were used in this study. Calves received colostrum and whole milk from their dams. The first blood sampling was performed before colostrum intake (day 0) and then at 1, 2, 7, 14 and 30 days of age. Blood serum was analyzed for the concentrations of haptoglobin (Hp), serum amyloid A (SAA), α1-acid glycoprotein (AGP), ceruloplasmin (Cp), and albumin (Alb). The results showed significant changes in the serum concentrations of Hp, SAA and Cp (P

The objective of this study was to describe the physiological changes in serum protein profile in calves during the first month of life. Seven clinically healthy calves were used in this study. Calves received colostrum and whole milk from their dams by voluntary sucking. The first blood sampling was performed within one hour after birth before colostrum intake (day 0) and then at 1, 2, 7, 14 and 30 days of age. Serum was analysed for total protein concentrations, and for the relative and absolute values of serum protein fractions – albumin, alpha1-(α1), alpha2-(α2), beta1-(β1), beta2-(β2) and gamma-(γ) globulins. The results showed a significant effect of age on total protein concentrations and for all the analysed protein fractions. The concentrations of total proteins, β2- and γ-globulins increased significantly one day after colostrum intake (P < 0.001) and then significantly decreased gradually till the end of the first month of age. An opposite trend was observed in the relative concentrations of al...

Respiratory diseases of cattle, particularly in young animals, represent the most important health and economic problem of cattle rearing. The aim of the present study was to evaluate the changes of selected blood indices in 25 calves aged 2–9 months suffering from etiologically undifferentiated chronic respiratory diseases. Blood samples were analysed for haematological indices and selected serum biochemistry variables. The results found in sick animals were compared with results from 25 healthy animals of the same age, housing and feeding system. Significant differences in means between the groups of clinically healthy and sick calves were found in 13 out of 24 evaluated indicators. In sick animals we found significantly higher mean concentrations of haemoglobin and total number of white blood cells (P < 0.05 and P < 0.01, respectively), as well as higher mean activity of AST and LDH (P < 0.01), concentrations of total proteins and total immunoglobulins (P < 0.001). Significantly lower mean values were recorded in the serum concentrations of albumin, creatinine and glucose (P < 0.001), as well as in the concentration of Mg (P < 0.01), P (P < 0.001), Fe and Zn (P < 0.05). The presented results suggest the effect of respiratory diseases in calves on several changes of haematological and selected serum biochemical indicators. They indicate that respiratory diseases did not lead only to direct disturbance of gas exchange and acid-base balance, but they also indirectly affect some other variables of blood biochemistry. Bovine, bronchopneumonia, blood, haematology, clinical biochemistry Respiratory diseases are the most prevalent disease in young cattle. Prophylactic measures, high cost of therapeutic interventions, mortality, reduced growth performance due to bovine respiratory disease (BRD), and irreversible pulmonary lesions lead to considerable economic losses (Coghe et al. 1999). Respiratory diseases in calves are associated with a wide scale of pathological findings in the lung parenchyma, as well as in the respiratory pathways. Although various forms of calf respiratory diseases are known, their clinical manifestation is frequently less differentiated. Despite the great variety of combinations of pathogens that have been implicated as causes of this disease, the clinical entity of most manifested is bronchopneumonia (Lekeux 1995). Cattle typically face two primary problems that contribute to a high incidence of BRD. First, stress associated with weaning and transportation has a negative effect on the immune system. Second, this stress typically occurs when the animal is exposed to a variety of infectious agents as a result of marketing (transporting) management procedures. Nutrition can interact with these two primary factors, most likely as a result of preweaning nutritional deficiencies or through decreased feed intake associated with stress. Low feed and thereby nutrient intake makes correction of nutritional deficiencies difficult, which could further compromise immune function and potentially increase susceptibility to infection (Cole 1996). Respiratory diseases lead to various degrees of hypoxaemia with possible subsequent tissue hypoxia. Other possible consequences include accompanying hypercapnia and respiratory acidosis (Wall 2001). Hypoxaemia and hypercapnia are the direct consequence of disturbances in basic respiratory functions, namely gas exchange. In calves suffering

Determination of the physiological electrophoretic patterns in animals is very useful for clinicians in diagnosing healthy and sick animals. The objective of this study was to investigate the serum protein electrophoretic pattern in cows, sheep, and goats in order to evaluate the differences in the size and number of protein fractions between the evaluated ruminant species. Ten adult multiparous high-yielding dairy cows, 10 adult female sheep and 10 adult female goats were included in this study. All the evaluated animals were clinically healthy. Serum was analyzed for total serum protein concentrations, and for the relative and absolute values of protein fractions with calculation of albumin/globulin ratios. Serum protein fractions were separated by zone electrophoresis on buffered agarose gel. Serum protein electrophoresis identified 6 distinct bands, comprising albumin, alpha1- (α1), alpha2- (α2), beta1- (β1), beta2- (β2), and gamma- (γ) globulins in cows. In sheep, serum proteins exhibited 6 fractions: albumin, α1-, α2-, β-, γ1- and γ2-globulins. In goats, serum proteins were separated into 5 fractions: albumin, α1-, α2-, β- and γ-globulins. Significant differences in the relative as well as absolute means were found for the albumin/globulin ratio and most of the protein fractions, except γ-globulins. No significant differences were found in the concentration of total proteins. These results describe the marked species differences in most of serum protein fractions between the evaluated groups of animals, and contribute to the current knowledge about the physiological electrophoretic pattern of serum proteins in ruminants, which can be used for diagnostic purposes.

Studies of the changes in serum protein pattern in the neonatal period in animals are still limited. Therefore, the objective of this study was to evaluate the changes in the concentrations of serum protein fractions in 7 clinically healthy merino lambs (4 males, 3 females) during their first month of life. The first blood sampling was performed before the colostrum intake and then at 1, 2, 7, 14 and 30 days of age. Blood serum was analysed for total serum protein concentrations and for the relative and absolute values of serum protein fractions - albumin, alpha1- (α1), alpha2- (α2), beta- (β), and gamma- (γ) globulins. The results showed a significant effect of age on the serum total protein concentrations and for all the protein fractions. The concentrations of total proteins and γ-globulins increased significantly 1 day after the colostrum intake (P< 0.001); then decreased gradually till the end of the 1st month. An opposite trend was observed in the concentrations of albumin. A significant decrease of values was found 1 day after the intake of colostrum (P< 0.001) with a subsequent progressive increase of values till the end of the evaluated period. The relative concentrations of α1-globulins significantly decreased during the first month of life (P< 0.001). On the other hand, the relative values of α2- and β-globulins increased significantly from birth till the end of the monitored period (P< 0.001). Our results suggest that the serum protein electrophoretic pattern in growing lambs is significantly influenced by the age of the evaluated animal, and this should be taken into consideration when interpreting the serum protein profile. Our findings extend existing knowledge about significant changes in the protein profile associated with the physiological adaptation process in the neonatal period in young animals.

We evaluated the effect of different storage conditions on the concentration of serum total proteins and their electrophoretic fractions in sheep. Blood samples were collected from 12 female Comisana sheep, and each serum obtained was divided into 4 aliquots. The first aliquot was analyzed immediately after separation (T0); the second was refrigerated at 4°C and analyzed after 24 h (T1), 48 h (T2), and 72 h (T3); the third was stored at −20°C immediately after centrifugation and analyzed after 2 days (T4); and the last aliquot was stored at −20°C after 24-h refrigeration and analyzed after 1 wk (T5). The concentrations of serum total proteins and their electrophoretic fractions (albumin, α-, β1-, β2-, and γ-globulins) was determined. A statistically significant ( p < 0.05) effect of storage conditions on all serum electrophoretic protein fractions and on the albumin-to-globulin (A/G) ratio was found. The values of albumin, α-globulins, and A/G ratio increased at T4 with respect to T0. The levels of α-globulins were higher at T1 than T0; the β1-globulins levels changed at T3, whereas the β2- and γ-globulins values as well as the A/G ratio changed at T2 and T3. At T4, we found an increase in the serum concentrations of albumin, α1-globulins, and on the A/G ratio, and a decrease of γ fraction. At T5, the concentration of α-globulins was higher than at T0. Hence, we recommend electrophoretic analysis of fresh ovine serum samples or of samples refrigerated for no more than 24 h to obtain accurate data.

The determination of serum proteins and their electrophoretic profiles is an important diagnostic aid in clinical biochemistry. Serum protein electrophoresis is a common technique of laboratory diagnosis in human, and has been studied intensively in small animal and equine medicine (Riond et al., 2009). However, in bovine medicine, the electrophoretic separation of serum proteins is a rarely used laboratory method. The pattern of serum protein electrophoresis results depends on the fractions of two major types of proteins: albumin and globulins. Many pathologic conditions can cause shifts in albumin and globulin concentrations (Keay and Doxey, 1982). Moreover, abnormalities of serum protein electrophoretic pattern must be interpreted in the view of the many other influences not associated with diseases. The age of evaluated animals is an important factor that may affect the concentrations of frequently analyzed biochemical variables, and may also influence the serum protein electrophoretic pattern.

In this study, we explain the need for more detailed laboratory diagnostic of serum proteins in veterinary medicine. The application of proteomic approaches over the last decade has provided new tools for clarifying the molecular aspects of physiological states, and for understanding the etiology and pathogenesis of many diseases. Proteomics performs large-scale protein analysis, describes the entire protein complement of a cell, tissue, biological fluid or organism and provides information on protein expression, localization, functions and interactions. Majority of plasmatic proteins is synthesized in hepatocytes, with albumin representing their largest quantitative part. The second major contributor is the imune system. Plasma proteins perform a nutritive function, exert colloidal osmotic pressure, and aid in the maintenance of acid-base balance. Individual proteins serve as enzymes, antibodies, coagulation factors, hormones, and transport substances. Fresh serum contains all of the plasma proteins except fibrinogen, factor V, and factor VIII. These are consumed during clot formation. The electrophoretic technique is the current standard of reference for the fractionation of the serum proteins in clinical biochemistry. Serum proteins determined by electrophoresis involves albumin, α1, α2, β1, β2 and γ-globulins. Individual blood serum proteins have different functions and their identification is used also as a diagnostic tool. Many of these proteins are the so-called acute phase proteins. For example, α1-acid glycoprotein concentration increases during inflammation or infection, as well as concentrations of other acute phase proteins (CRP, serum amyloid A protein, α1-antitrypsin, haptoglobin, ceruloplasmin and fibrinogen) based on increased synthesis of hepatocytes with subsequent release of these proteins in blood. Alfa1-antitrypsin, member of the superfamily of proteinase inhibitors, has a crucial effect on inactivation of neutrophil elastase and other proteases, which maintains protease–antiprotease balance. Ceruloplasmin takes part in copper metabolism and its decreased plasmatic concentration is associated with copper deficiency. Concentrations of serum proteins are influenced by many physiological (age, pregnancy, lactacion etc.) and pathological (malnutrition, renal and hepatal diseases etc.) factors. Current widespread use of electrophoresis is commensurate with its reflection of a variety of changes in serum protein patterns in disease in different species of animals.