Serum protein electrophoresis in healthy and injured southern white rhinoceros (Ceratotherium simum simum)

Abstract

Investigation of globulin fractions by serum protein electrophoresis (SPE) is the first step towards evaluation of the proteome in the southern white rhinoceros (Ceratotherium simum simum). Furthermore, identification of changes in globulins in animals with poaching and other injuries can guide discovery of potentially useful biomarkers of inflammation. The aim of this study was to develop reference intervals for agarose gel SPE in healthy white rhinoceros and to compare these serum protein electrophoresis results to those from animals with tissue trauma. Reference intervals for total serum protein and agarose gel electrophoretic albumin and globulin fractions were generated using serum samples from 49 healthy free-ranging adult white rhinoceros. A standardised gating system together with identification of specific proteins by mass spectrometry aided in fraction identification. Six globulin fractions were identified: α1a, α1b, α2, β1, β2 and γ. Reference intervals were generated for total serum protein (76–111 g/L), albumin (10–27 g/L) and globulin fractions (α1a: 1.6–3.2 g/L; α1b: 1.7–3.6 g/L; α2: 16.1–26.6 g/L; β1: 6.6–18.2 g/L; β2: 11.8–30.4 g/L; γ: 10.4–23.1 g/L; albumin: globulin ratio: 0.12–0.39). Results were compared to those from 30 animals with various degrees and chronicities of tissue trauma. Wounded animals had lower concentrations of total serum protein, albumin, total globulin, α and β1 globulins, lower percentages of α2 and β1 globulins, and higher percentages of β2 and γ globulins. These protein changes are similar to those seen in human patients with wounds rather than classic acute phase or chronic inflammatory responses.

Modulatory effect of lipopolysaccharide on immune‐related gene expression and serum protein fractionation in grey mullet,Mugil cephalus

“…Polyacrylamide gel electrophoresis was taken as a biomarker for many immunological and toxicological studies (Muhammad et al, 2018). Profiling of serum proteins facilitates identification of many issues related to diseases and inflammation in mammals and fish (Akbary & Jahanbakhshi, 2018;Hooijberg et al, 2018;Yang, Cho, Wang, Park, & Yang, 2016). Serum protein usually separates into albumin and globulins fractions: α1, α2, β1, β2 and γ according to their sizes and electrical charges (Christiansen et al, 2015;Jenkins, 1999).…”

Inflammatory and oxidative status in European captive black rhinoceroses: a link with Iron Overload Disorder?

“…In this study, selecting captive WR instead of free-ranging BR as the negative control precisely aimed at limiting the captivity bias since captivity may be pro-inflammatory by itself [37,53]. Serum protein electrophoretic results of the captive WR included in this study showed some variations in comparison to healthy free-ranging WR [31], further underlining the interest of selecting captive WR as a control group in order to limit the captivity bias. Obesity is described for being pro-oxidative and pro-inflammatory [54], but no study to date investigates the consequences of overweight in rhinoceroses.…”

“…Inflammation status was evaluated by measuring total serum protein (TP, biuret method) and agarose gel electrophoretic albumin and globulin fractions (albumin and globulins including α 1 -, α 2 -, β- and γ-globulin fractions, agarose gel method (Hyrys2, Hydragel; Sebia, Evry, France). Globulin fractions were determined according to recent published data from Hooijberg and colleagues [31]. α 1 -globulins refers to α 1 -a and α 1 -b fractions, and β-globulins refers to β1 and β2 fractions.…”

Protein characterization using electrophoresis and immunofixation; a case‐based review of dogs and cats

“…Among these is the general rule that the α‐2/β‐1 demarcation typically lies at approximately the halfway point of the electrophoretogram . Calculation of relative migration distance has been advocated to help determine peaks and demarcation points between fractions . The relative migration distance reportedly allows a degree of standardization between different electrophoretic runs and can be calculated using the equation…”

“…In most settings, chemically determined albumin is expected to be higher than densitometric albumin, due to binding of the bromocresol green dye to α‐ and β‐globulins . Additionally, some albumin has been shown to electrophoretically migrate in the globulin fraction of several species . M‐proteins can cause a significant falsely increased or decreased colorimetric albumin concentration, and in cases where the M‐protein is not soluble under the conditions of the total protein measurement, M‐proteins can cause falsely decreased total protein measurements (Figure ) …”