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1.
J Wildl Dis ; 58(3): 670-674, 2022 07 01.
Artigo em Inglês | MEDLINE | ID: mdl-35417920

RESUMO

The ketone ß-hydroxybutyrate (BHB) serves as an energy source when bodily energy stores are low. Concentrations of this blood analyte are often determined by spectrophotometric quantitative assays with a dry chemistry analyzer; however, rapid assessment with point-of-care devices have the potential to improve assessment of animals in the field or in clinical settings. We measured BHB concentrations in whole blood samples from 54 leatherback (Dermochelys coriacea), 27 loggerhead (Caretta caretta), and 14 green (Chelonia mydas) sea turtles in Florida, US with a point-of-care device and validated its use with corresponding plasma samples and dry chemistry analyzer as the gold standard. Concentrations of BHB highly correlated between the two methods for all three species, with loggerheads showing the best agreement and lowest bias. Therefore, the point-of-care device used for this study (Lucidplus ß-ketone monitoring system) is probably appropriate for sea turtle BHB measurements.


Assuntos
Tartarugas , Ácido 3-Hidroxibutírico , Animais , Florida , Sistemas Automatizados de Assistência Junto ao Leito
2.
J Zoo Wildl Med ; 51(1): 123-130, 2020 Mar 17.
Artigo em Inglês | MEDLINE | ID: mdl-32212555

RESUMO

Agarose gel electrophoresis (AGE) has been widely implemented throughout veterinary medicine and for analysis of plasma proteins of avian and reptile species. Capillary zone electrophoresis (CZE) is becoming a standard method in human clinical pathology laboratories but has not widely been used for the analysis of animal samples. The objective of the present study was to compare protein fractions derived from AGE and CZE methods using plasma from the green turtle (Chelonia mydas). Plasma samples were analyzed by AGE and CZE per manufacturer guidelines. The methods were assessed by CV analysis, Spearman's correlation, Passing-Bablok regression, and Bland Altman plots. CZE consistently resolved more fractions than AGE with three fractions observed in the prealbumin migrating region versus one for AGE and two fractions in the γ globulin region versus one for AGE. Compared with AGE, CZE showed a lower CV in intra-assay tests (1.0-4.9% vs 2.0-28.3%) and a lower or overlapping CV in interassay tests (1.0-10.6 vs 2.3-22.0). The prealbumin, α2 globulin, and ß globulin fractions correlated the least between the methods (for all three fractions: rs ≤ 0.28, P > 0.21). Moderate, significant correlations between AGE and CZE methods were observed for albumin (rs = 0.78, P < 0.0001) and γ globulins (rs = 0.78, P < 0.0001). CZE has a higher precision and ease of use over AGE and offers the opportunity to resolve additional protein fractions. This will necessitate the development of new conventions in placement of fraction delimits, definition of species-specific reference intervals, and evaluation of clinical utility in abnormal turtles.


Assuntos
Eletroforese das Proteínas Sanguíneas/veterinária , Eletroforese em Gel de Ágar/veterinária , Eletroforese Capilar/veterinária , Plasma/química , Tartarugas/sangue , Animais , Eletroforese das Proteínas Sanguíneas/métodos , Proteínas Sanguíneas/análise , Eletroforese em Gel de Ágar/métodos , Eletroforese Capilar/métodos , Especificidade da Espécie
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