Electrophoretic serum protein fraction profile during the different physiological phases in Comisana ewes

The aim of this study was to evaluate the influence of different physiological phases on serum total proteins and their fractions of ten Comisana ewes housed in Mediterranean area. From each animal, blood samples were collected at different physiological phases: late pregnancy, post-partum, early, mid-, end lactation and dry period. On all samples serum total proteins were determined by the biuret method, and albumin, α-globulins, β(1) -globulins, β(2) -globulins and γ-globulins concentrations were assessed using an automated system. One-way repeated measures analysis of variance was applied to determine the significant effect of different physiological phases on the parameters studied. During the late pregnancy and post-partum, total proteins, β1- and β2-globulins and γ-globulins showed the highest values. Starting from post-partum, α-globulins increased to reach their peaks in mid-lactation. Early lactation was characterized by low γ-globulins values. The increase in serum albumin concentration and the drop in some globulin fractions determined the significant increase in albumin/globulin ratio. The obtained results contributed to improve the knowledge on electrophoretic profile during the different physiological phases in ewes, confirming that pregnancy and lactation periods affect the protein metabolism. Particularly, serum protein fractions pattern could give information about dehydration, plasma volume expansion and hepatic function, which occur during the different physiological phases. Dynamics of the protein profile - from pregnancy to dry period - which are provided by our results, could be considered as guidelines for the management strategies to guarantee the nutritional needs of these animals during the different physiological phases and to avoid a decline of productive performance and consequently an economic loss.     

Serum protein concentrations from clinically healthy horses determined by agarose gel electrophoresis

Background: Serum protein electrophoresis is a useful screening test in equine laboratory medicine. The method can provide valuable information about changes in the concentrations of albumin and α‐, β‐, and γ‐globulins and thereby help characterize dysproteinemias in equine patients. Reference values for horses using agarose gel as a support medium have not been reported. Objectives: The purpose of this study was to establish reference intervals for serum protein concentrations in adult horses using agarose gel electrophoresis and to assess differences between warm‐blooded and heavy draught horses. In addition, the precision of electrophoresis for determining fraction percentages and the detection limit were determined. Methods: Blood samples were obtained from 126 clinically healthy horses, including 105 Thoroughbreds and 21 heavy draught horses of both sexes and ranging from 2 to 20 years of age. The total protein concentration was determined by an automated biuret method. Serum protein electrophoresis was performed using a semi‐automated agarose gel electrophoresis system. Coefficients of variation (CVs) were calculated for within‐run and within‐assay precision. Data from warm‐blooded and draught horses were compared using the Mann–Whitney U test. Results: Within‐run and within‐assay CVs were <5% for all protein fractions. No significant difference was found between warm‐blooded and heavy draught horses and so combined reference intervals (2.5–97.5%) were calculated for total protein (51.0–72.0 g/L), albumin (29.6–38.5 g/L), α₁‐globulin (1.9–3.1 g/L), α₂‐globulin (5.3–8.7 g/L), β₁‐globulin (2.8–7.3g/L), β₂‐globulin (2.2–6.0 g/L), and γ‐globulin (5.8–12.7 g/L) concentrations, and albumin/globulin ratio (0.93–1.65). Conclusion: Using agarose gel as the supporting matrix for serum protein electrophoresis in horses resulted in excellent resolution and accurate results that facilitated standardization into 6 protein fractions.     

Electrophoretic patterns of serum proteins in blue foxes with special reference to changes associated with nosematosis.

The serum proteins in 1 group of healthy breeders, 1 group of healthy pups and 4 groups of foxes suffering from various diseases were separated electrophoretically on cellulose acetate membranes. In most of the sera, the proteins were separated into 1 albumin fraction and 5 globulin fractions designated alpha₁, alpha₂, alpha₃, beta and gamma. The mean concentrations of the total proteins and the various serum fractions in the disease groups were compared statistically with the mean values of the normal groups.A nosematosis group was characterized by a distinct hypergammaglobulinaemia together with an increase in the total protein — and a decrease in the albumin concentrations. However, in 2 cubs recovering from nosematosis the hypergammaglobulinaemia was shown to be reversible.In a feed intoxication group the concentration of albumin was found to be lower and the alpha₃-globulin higher than the corresponding values in the healthy group. A virus hepatitis group was characterized by a decrease in the concentrations of albumin and beta-globulin and an increase in the alpha₁- and alpha₃-globulins. In the toxoplasmosis group the total protein and alpha₁- and alpha₃-globulins showed concentrations below the normal values.     

Serum protein electrophoretic pattern in young and adult camels

OBJECTIVE: To compare the electrophoretic pattern of serum proteins in clinically healthy adult camels (between 3 and 8 years of age) and camel calves (less than 3 months of age). DESIGN: Laboratory analysis of serum from healthy camels. PROCEDURE: Blood was collected from 30 healthy adult camels and 30 camel calves and the serum separated. Total protein of each serum sample was estimated by automated chemistry analyser. The proteins were fractionated by automated electrophoresis on agarose gel. RESULTS: Serum proteins migrated on the agarose gel as one albumin, two alpha (alpha1 and alpha2-globulins), two beta (beta1 and beta2-globulins) and one gamma-globulin fractions. In adult camels the mean concentration of total protein, albumin alpha1, alpha2, beta1, beta2 and gamma-globulins was 56.8 +/- 1.5, 30.7 +/- 0.8, 2.4 +/- 0.1, 3.2 +/- 0.1, 9.7 +/- 0.3, 3.4 +/- 0.2 and 8.6 +/- 0.3 g/L, respectively. These values in calves were 49.7 +/- 1.8, 23.7 +/- 0.8, 3.2 +/- 0.2, 3.1 +/- 0.2, 14.2 +/- 0.2, 4.0 +/- 0.2 and 4.1 +/- 0.2 g/L, respectively. CONCLUSION: The concentration of total proteins, albumin and gamma-globulins was higher (P < 0.05) in the adult camels than in camel calves. The concentrations of beta1 globulins was higher (P < 0.05) in calves as compared to adult camels.     

Analysis of serum proteins in clinically healthy goats (Capra hircus) using agarose gel electrophoresis

Background: Electrophoretic patterns of serum proteins provide useful information on pathological conditions in ruminants. Their reference values, however, are dissimilar to those of other species. Reference values for goats using agarose gel as the supporting matrix have not been reported. Objective: The aim of this study was to evaluate serum concentrations of total protein and protein fractions (albumin and globulins) by means of agarose gel electrophoresis (AGE) in goats in order to establish electrophoretic reference intervals and to evaluate potential changes associated with aging. Methods: Blood was collected from 105 clinically healthy Girgentana goats by means of jugular venipuncture. Serum protein concentrations were assessed by AGE. Three age groups were compared: 1–1.5 years, 2–4 years, and 5–12 years. Results: Values (mean ± SD) were determined for concentrations of total protein (72.26 ± 6.40 g/L), albumin (31.80 ± 4.00 g/L), α‐globulins (6.40 ± 1.23 g/L), β₁‐globulins (10.50 ± 2.58 g/L), β₂‐globulins (5.18 ± 1.60 g/L), and γ‐globulins (18.65 ± 5.90 g/L) and for albumin/globulin (A/G) ratio (0.82 ± 0.20). One‐way ANOVA showed statistically significant age‐related differences for total protein and α‐globulin concentrations and A/G ratios. Age influenced protein concentrations with the 5–12‐year‐old group having higher total protein and α‐globulin concentrations and lower albumin concentration and A/G ratios than the 2–4‐year‐old group. Conclusions: This study provides reference values for total protein concentrations and protein fractions obtained by AGE in goats. Some values vary with age. Age‐specific reference intervals are reported in order to provide clinicians with an additional diagnostic aid.     

引入青海的亚发蛋鸡血清蛋白质指标的测定

采用折射计法和醋酸纤维薄膜电泳法对５９２６４部队养殖场的３１只亚发蛋鸡的血清蛋白质指标进行了测定。结果：血清总蛋白，８０．５２±１２．６９ｇ／Ｌ；白蛋白，３０．５４±６．４８ｇ／Ｌ球蛋白，４９．９８±９．７４ｇ／Ｌ。血清蛋白质组分（％）：白蛋白，３６．７６±４．７９；ａ－球蛋白，１０．３８±２．６２；β－球蛋白，１６．０１±２．９９；γ－球蛋白，３６．８５±５．１８；Ａ／Ｇ，０．６４±０．２１。     

Association Between Low Serum Zinc Concentration and Hypogammaglobulinemia in Foals of Different Age Categories

Zinc (Zn) is an essential trace element, and its deficiency causes defects in the response of the immune system, affecting the synthesis and secretion of γ-globulins. In this study, we evaluated serum Zn levels in race foals of different age categories to establish the relationship between subnormal values of Zn and decreased levels of γ-globulins. Decreased γ-globulin levels were accompanied by total protein and albumin serum levels that were within the normal range for the species. Serum Zn was measured in 304 foals (aged between 8 and 24 months), which were classified into three categories (weaning, yearling, and 2 years). The albumin/globulin ratio was 1.28 ± 0.2964 in the normal Zn group and 2.185 ± 0.818 (P < .001) in the low Zn group. Hypogammaglobulinemia was found to be more frequent in the yearling and in the 2-year-old category animals (P < .001 low Zn vs. normal Zn).     

Studies of composition and major protein level in milk and colostrum of mares

The aim of the study was to determine the changes in composition and physicochemical features (pH, density, thermostability and acidity) of mare colostrum and milk, and of protein fraction contribution (serum albumin, β-casein, γ-casein, α-lactalbumin, G class immunoglobulins) depending on lactation stage. The research material was colostrum and milk samples from 12 Arabian mares. Colostrum samples were collected within 2 h after parturition and milk samples were collected twice, in the 3rd and 6th weeks of lactation. The level of basic milk components decreased significantly (only lactose content increased) as compared to colostrum. Total bacteria count and somatic cell count decreased significantly with an increase in resistance and urea level. The changes observed were connected to differentiated contribution of particular protein fractions and their relative proportions. Lower levels of γ-casein (P ≤ 0.05), β-casein, serum albumin as well as α-lactalbumin were observed in colostrum as compared to those in milk. Any relationship between lactation stage and β-casein content was observed. Serum albumin and α-lactalbumin content increased in subsequent milkings. The level of G class immunoglobulins decreased significantly and its highest level was noted in colostrum. Any significant differences between the 3rd and 6th lactation weeks were obtained.     

Effect of storage time and temperature on the total protein concentration and electrophoretic fractions in equine serum

Serum protein electrophoresis (SPE) is a technique that could be considered one of the most useful diagnostic aids available to the clinician. The effect of storage time and temperature on the total proteins and electrophoretic fractions (albumin, α₁-, α₂-, β₁-, β₂-, and γ-globulins) was assessed in 24 healthy horses. All samples, collected by jugular vein puncture, were centrifuged and divided into 4 aliquots. The 1st aliquot was analyzed within 3 h from collection (time 0), the 2nd was refrigerated at +4°C for 24 h, the 3rd was refrigerated at +4°C for 48 h, and the last was frozen at −20°C for 48 h. One-way repeated-measures analysis of variance (ANOVA) showed a significant effect (P < 0.05) of the different storage conditions on the concentrations of all the parameters studied and significant variations in the percentages of albumin, α₁-globulins, α₂-globulins, and γ-globulins. Compared with time 0 the total protein concentration increased significantly after 48 h at −20°C, the albumin percentage decreased after 48 h at −20°C, the α₁-globulin percentage increased after 24 h at +4°C, the α₂-globulin percentage increased after 48 h at +4°C and at −20°C, and the γ-globulin percentage increased after 48 h at −20°C. The results should help veterinary practitioners handle and store equine serum samples appropriately. Further investigations at different storage times and temperatures could be useful.     

Comparison of four methods for determination of total protein concentrations in pleural and peritoneal fluid from dogs

OBJECTIVE: To compare 4 techniques for determination of total protein concentrations in peritoneal and pleural effusions from dogs. SAMPLE POPULATION: 23 peritoneal and 12 pleural fluid samples from 35 dogs with various abnormalities. PROCEDURE: Samples were collected into tubes containing EDTA, centrifuged, and stored at -20 C until total protein concentrations were assessed. Protein concentration in each sample was determined by use of urine test strips, refractometry, and Bradford and biuret techniques. Accuracy of each method was determined, using dilutions of human control sera. RESULTS: There was good correlation among results of all quantitative procedures. Results of the biuret technique were more accurate than results of the Bradford assay. Refractometry underestimated protein concentration in samples with < 20 g of protein/L. Results of urine test strips correctly classified effusion samples into 2 groups on the basis of total protein concentrations less than or greater than 20 g/L. CONCLUSIONS AND CLINICAL RELEVANCE: Results of any of these 4 techniques can be used to rapidly and efficiently differentiate peritoneal and pleural fluid from dogs into transudates and exudates on the basis of total protein concentration less than or greater than 20 g/L, respectively.     

Fecal alpha1-proteinase inhibitor concentration in dogs with chronic gastrointestinal disease

Background: Fecal α₁‐proteinase inhibitor (α₁‐PI) clearance is a reliable, noninvasive marker for protein‐losing enteropathy in human beings. An assay for use in dogs has been developed and validated. Objective: The aim of this study was to evaluate fecal α₁‐PI concentration in dogs with chronic gastrointestinal disease, compared with healthy dogs, and to assess its correlation with serum albumin concentration. Methods: Fecal samples were collected from 2 groups of dogs. Group 1 consisted of 21 clinically healthy client‐owned dogs without signs of gastrointestinal disease. Group 2 consisted of 16 dogs referred for investigation of suspected gastrointestinal disease. On the basis of gastric and duodenal biopsies, group 2 was further subdivided into dogs with normal histology (n = 9) and those with histologic abnormalities (n = 7: inflammatory bowel disease, n = 3; lymphangiectasia, n = 4). An ELISA was used to measure α₁‐PI concentrations in fecal extracts. Results: Fecal α₁‐PI concentrations, expressed as μg/g of feces, were not significantly different between groups 1 and 2 as a whole. However, fecal α₁‐PI concentrations (median, minimum‐maximum) were significantly higher in dogs with gastrointestinal diseases associated with histologic abnormalities (60.6 μg/g, 7.4–201.7 μg/g) compared with dogs with normal histology (3.8 μg/g, 0.7–74.0 μg/g) and control dogs (9.9 μg/g, 0.0–32.1 μg/g). There was no significant correlation between fecal α₁‐PI and serum albumin concentrations in dogs with gastrointestinal disease. Conclusions: Increased fecal α₁‐PI concentration may signal the need to obtain gastrointestinal biopsies for a final diagnosis. Fecal α₁‐PI concentration may be a useful test for early detection of protein‐losing enteropathy before decreases in serum albumin concentration can be detected.     

九龙藏黄牛乳蛋白的组成及遗传多态性研究

本研究旨在了解生活在高海拔地区的藏黄牛乳的生化组成特点。试验测定了43头九龙藏黄牛乳蛋白含量、乳蛋白组成和酪蛋白多态性。藏黄牛乳蛋白含量低,仅约为29 g/L;电泳分析结果显示,脱脂乳蛋白组成与普通牛乳接近,主要包括酪蛋白、α-乳清蛋白和β-乳球蛋白等组分,β-Lg与α-La含量的比值低于牦牛;酪蛋白的相对含量约为70%,主要包含α_s-CN和β-CN,二者分别检测到3和2种基因型。研究结果表明,九龙藏黄牛乳的组成与生活在类似生态环境中的九龙牦牛存在差异。     

The pharmacokinetics of nitazoxanide active metabolite (tizoxanide) in goats and its protein binding ability in vitro

Zhao, Z., Xue, F., Zhang, L., Zhang, K., Fei, C., Zheng, W., Wang, X., Wang, M., Zhao, Z., Meng, X. The pharmacokinetics of nitazoxanide active metabolite (tizoxanide) in goats and its protein binding ability in vitro. J. vet. Pharmacol. Therap. 33 , 147–153. The pharmacokinetics of tizoxanide (T), the active metabolite of nitazoxanide (NTZ), and its protein binding ability in goat plasma and in the solutions of albumin and α‐1‐acid‐glycoprotein were investigated. The plasma and protein binding samples were analyzed using a high‐performance liquid chromatography (HPLC) assay with UV detection at 360 nm. The plasma concentration of T was detectable in goats up to 24 h. Plasma concentrations vs. time data of T after 200 mg/kg oral administration of NTZ in goats were adequately described by one‐compartment open model with first order absorption. As to free T, the values of t_1/2Ka, t_1/2Ke, T_max, C_max, AUC, V/F_(c), and Cl_(s) were 2.51 ± 0.41 h, 3.47 ± 0.32 h, 4.90 ± 0.13 h, 2.56 ± 0.25 μg/mL, 27.40 ± 1.54 (μg/mL) × h, 30.17 ± 2.17 L/kg, and 7.34 ± 1.21 L/(kg × h), respectively. After β‐glucuronidase hydrolysis to obtain total T, t_1/2ke, C_max, T_max, AUC increased, while the V/F_(c) and Cl_(s) decreased. Study of the protein binding ability showed that T with 4 μg/mL concentration in goat plasma and in the albumin solution achieved a protein binding percentage of more than 95%, while in the solution of α‐1‐acid‐glycoprotein, the percentage was only about 49%. This result suggested that T might have much more potent binding ability with albumin than with α‐1‐acid‐glycoprotein, resulting from its acidic property.     

Live Weight Estimation of Donkeys in Central México from Measurement of Thoracic Circumference

Body measurements (length from nape of neck to the withers; height to withers; length from withers to tail root; length from shoulder to tuber ischii; thoracic circumference; umbilical circumference) were taken and correlated with live weight from 160 donkeys (mean ± standard deviation = 6 ± 2.6 years old) in Central México. The age was assessed from dentition. Sex of the donkeys was also recorded. Sex was an important factor of variation (p = 0.011). Live weight was estimated using two allometric models. Model 1: Live weight = β _o × (thoracic circumference)^β1. Model 2: Live weight = β _o × (height to the withers) ^βl × (thoracic circumference) ^β2. Separate prediction equations were produced for males and females, plus one for the total sampled. The ‘best fit’ models, were those using thoracic circumference to predict the live weight. Males: live weight = 0.018576 × (thoracic circumference)^1.84107 (R ² = 0.9839). Females: live weight = 0.031255 × (thoracic circumference)^1.72888 (R ² = 0.9839). The equations derived to estimate the live weight of donkeys in Britain, Morocco and Zimbabwe were less satisfactory for use with donkeys from Central México because they overestimated the live weight.     

Cellulose acetate electrophoresis of canine plasma after fibrinogen precipitation by ethanol

Background: In routine canine medicine, anticoagulated blood is often the only sample sent to laboratories for diagnostic purposes. This hampers the interpretation of protein electrophoretic tracings because plasma contains fibrinogen, which migrates in the β–γ region. In human medicine, fibrinogen can be precipitated from plasma using ethanol. Objectives: The purpose of this study was to assess ethanol precipitation as a method for removing fibrinogen from canine plasma so as to facilitate the interpretation of electorphoresis results. Methods: Blood samples collected from 40 dogs were divided into plain tubes and tubes containing EDTA (n=20) or lithium–heparin (n=20). An aliquot of plasma from each sample was incubated with ethanol at a final concentration of 100 mL/L. Cellulose acetate electrophoresis was then performed on serum, plasma, and plasma treated with ethanol. To verify the efficiency of ethanol treatment, fibrinogen was added to 5 canine serum samples at final concentrations of 2.5, 5.0, and 10.0 g/L, and electrophoresis was performed before and after ethanol treatment. Results: Visual analysis of electrophoretograms from ethanol‐treated samples confirmed the disappearance of the fibrinogen peak from the β₂‐globulin region. Treatment with ethanol caused a significant decrease in the percentage of β₂‐globulins and a significant increase in the percentage of α₂‐globulins. Absolute values of most electrophoretic fractions were significantly decreased in ethanol‐treated plasma compared with serum. Conclusions: Ethanol treatment successfully removed fibrinogen from canine plasma and normalized electrophoretic profiles, but probably also precipitated proteins other than fibrinogen. Ethanol treatment is recommended to facilitate visual identification of abnormal monoclonal peaks, but not for determining absolute protein concentrations in electrophoretic fractions.     

Use of refractometry for determination of psittacine plasma protein concentration

Background: Previous studies have demonstrated both poor and good correlation of total protein concentrations in various avian species using refractometry and biuret methodologies. Objectives: The purpose of the current study was to compare these 2 techniques of total protein determination using plasma samples from several psittacine species and to determine the effect of cholesterol and other solutes on refractometry results. Methods: Total protein concentration in heparinized plasma samples without visible lipemia was analyzed by refractometry and an automated biuret method on a dry reagent analyzer (Ortho 250). Cholesterol, glucose, and uric acid concentrations were measured using the same analyzer. Results were compared using Deming regression analysis, Bland–Altman bias plots, and Spearman's rank correlation. Results: Correlation coefficients (r) for total protein results by refractometry and biuret methods were 0.49 in African grey parrots (n=28), 0.77 in Amazon parrots (20), 0.57 in cockatiels (20), 0.73 in cockatoos (36), 0.86 in conures (20), and 0.93 in macaws (38) (P≤.01). Cholesterol concentration, but not glucose or uric acid concentrations, was significantly correlated with total protein concentration obtained by refractometry in Amazon parrots, conures, and macaws (n=25 each, P<.05), and trended towards significance in African grey parrots and cockatoos (P=.06). Conclusions: Refractometry can be used to accurately measure total protein concentration in nonlipemic plasma samples from some psittacine species. Method and species‐specific reference intervals should be used in the interpretation of total protein values.     

Comparison of milk protein composition in a Swedish and a Danish dairy herd using reversed phase HPLC

Abstract

The milk composition in a Swedish herd, consisting of Swedish Red and White cows (SRB) and Swedish Holstein cows (SLB), and in a Danish herd, consisting of Danish Holstein-Friesian cows (SDM), was evaluated. Concentrations of the major milk proteins (κ-casein, α_S1-casein, β-casein, β-lactoglobulin A, β-lactoglobulin B and α-lactalbumin) of 134 individual milk samples were determined by reversed phase (RP) HPLC. Other parameters determined included milk fat, urea, lactose, calcium, lactoferrin, somatic cell count and protein degradation (determined as level of free amino-terminals). Analysis of variance was used to compare concentrations of analysed milk variables between SRB and SLB or between SLB and SDM. Concentration of total protein, total casein, β-casein and κ-casein were significantly higher in SRB milk compared with SLB milk. Concentration of α-lactalbumin and calcium were significantly higher in SDM milk than in SLB milk. The concentration of urea was higher in SLB than in SDM milk and is suggested to reflect differences in feeding regimes between the investigated Swedish and Danish herd.     

蒺藜皂苷对体外瘤胃发酵的影响

试验旨在利用人工瘤胃双外流连续培养系统,初步研究日粮中添加不同浓度(0、0.15、0.30、0.60 g/L)蒺藜皂苷(GSTT)对反刍动物瘤胃发酵参数的影响。结果表明,日粮添加不同水平GSTT对瘤胃pH、总挥发性脂肪酸(TVFA)浓度无显著影响(P>0.05);随着GSTT添加水平的提高,人工瘤胃液内NH₃-N浓度、乙酸摩尔比例和乙酸/丙酸比例显著降低(P<0.05),丙酸摩尔比例显著升高(P<0.05)。提示,GSTT可望作为一种潜在的反刍动物瘤胃发酵调控剂来改变瘤胃发酵模式,改善对饲料能量和蛋白质的利用效率。综合考虑,0.30 g/L GSTT为较适宜添加量。     

Identification of apolipoprotein A‐I in the α‐globulin fraction of avian plasma

Background: Plasma protein electrophoresis is frequently used in birds as a tool for the diagnosis and monitoring of disease. Identification of proteins in individual peaks can help improve our understanding of changes in protein concentration in physiologic and pathologic conditions. Objective: The aim of this study was to verify the presence and identity the protein(s) in the prominent α‐globulin peak of orange‐winged parrots (Amazona amazonica), black kites (Milvus migrans), and rock pigeons (Columba livia). Methods: Heparinized plasma samples were obtained from 12 birds of each species. Agarose gel electrophoresis and total protein concentration were determined using standard techniques. One plasma sample from each species was then electrophoresed using high‐resolution agarose gels to isolate the α‐globulin band. Gel strips were digested in trypsin and peptides were extracted and analyzed using liquid chromatography with tandem mass spectrometry. De novo sequencing was used to identify the protein based on homology scoring against a protein database. Results: Electrophoresis verified the presence of a single prominent α‐globulin peak, usually in the α₁‐region, that had a median concentration of 9.4 g/L (range, 2.1–11.7 g/L, 21.6% of total protein) in parrots, 12.2 g/L (10.4–13.2 g/L, 35.9%) in kites, and 10.7 g/L (9.0–11.5 g/L, 40.0%) in pigeons. Mass spectrometry and sequencing analysis unequivocally identified the protein as a mature circulating form of apolipoprotein A‐I (apo A‐I) in all 3 species. Conclusions: Apo A‐I accounts for the prominent α‐globulin peak and comprises a major proportion of total protein concentration in diverse avian species. As a high‐density lipoprotein and negative acute phase protein with a pivotal role in cholesterol homeostasis, further study is warranted to determine the significance of changes in apo A‐I concentration in avian electrophoretograms.