A simple colorimetric method for determination of serum triglycerides with lipoprotein lipase and glycerol dehydrogenase

Sugiura, Masahiro; Oikawa, Tsutomu; Hirano, Kazuyuki; Maeda, Hitoshi; Yoshimura, H.; Sugiyama, Masayasu; Kuratsu, T

doi:10.1016/0009-8981(77)90003-1

Cited by 53 publications

(6 citation statements)

References 15 publications

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“…Immunoglobulin electrophoresis was performed as described by Henry et al (1974). The total serum cholesterol was measured according to Mamoru et al (1977). The serum triglyceride concentrations were measured according to Izzo et al (1981).…”

Section: Biochemical Studiesmentioning

confidence: 99%

Comparison between Biochemical Analysis of Cattle Amniotic Fluid and Maternal Serum Components during Pregnancy.

Essawi¹,

Mostafa²,

Shorbagy³

2020

jwpr

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The present study aimed to compare the biochemical components including Total Protein (TP), albumin, globulins, cholesterol, triglycerides, High and Low-Density Lipoproteins (HDL and LDL), creatinine, urea, sodium (Na), potassium (K), chloride (Cl), calcium (Ca) and inorganic phosphorus (P), of Amniotic Fluid (AF) with those of Maternal Serum (MS) during the first, second and third trimesters of pregnancy in cattle and Fetal Serum (FS) at birth. At birth AF, MS and FS were collected. Maternal blood samples and gravid uteri were collected after accidental slaughter. The actual data recorded during three trimesters according to the curved crown-anus length of the fetus. The MS concentrations of globulins, cholesterol, triglycerides, lipoproteins, creatinine, Na, K, Cl, Ca and inorganic-P were significantly higher than the AF during the first trimester. At delivery, the concentrations of cholesterol, triglycerides, and creatinine in the AF were lower than those in the MS or FS. The concentrations of Ca and inorganic-P in the FS were higher than those in the MS or AF. The levels of TP, creatinine, urea in the AF and urea in the MS increased as the gestation stages advanced. The levels of Na and Ca in the AF decreased as the gestation stage advanced while the K concentration increased. In conclusion, our results indicated an active placental transport for Ca and P. The TP, albumin, globulins, cholesterol, triglycerides, HDL and LDL, creatinine, urea, Na, K, Cl, Ca and P in AF and MS during the first, second and third trimesters of pregnancy in cattle might be changed with progressing the gestation.

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Section: Biochemical Studiesmentioning

confidence: 99%

Comparison between Biochemical Analysis of Cattle Amniotic Fluid and Maternal Serum Components during Pregnancy.

Essawi¹,

Mostafa²,

Shorbagy³

2020

jwpr

View full text Add to dashboard Cite

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“…At present, with the rapid advancement of science and technology, cutting-edge equipment has been developed for the detection of TGs. These include colorimetry [8,9], spectrophotometry [10][11][12][13][14], chromatography [15,16], fluorometry [17], titrimetry [18], nuclear magnetic resonance [19], and enzymatic colorimetry [20]. Nevertheless, most of this mainstream equipment operates in a timeconsuming and expensive fashion, not to mention requiring highly skilled technicians.…”

Section: Introductionmentioning

confidence: 99%

Construction of a Hydrogel Pectin-Based Triglyceride Optical Biosensor with Immobilized Lipase Enzymes

Hasanah

Sani²,

Heng

et al. 2019

Biosensors

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A novel and simple optical biosensor to detect triglycerides (TGs) has been successfully constructed by using pectin hydrogel membrane as the indicator pH and chromoionophore ETH 5294 (CI), with lipase as the catalyst. The enzymatic working system against TGs releasing H+ ions will affect the color absorbance of CI. The characterization results show that a TG biosensor has the optimum condition and sensitivity at the phosphate buffer concentration of 50 mM, pH 7, and enzyme loading of 60 μg. The biosensor works at the tripalmitin (TP) concentration range of 100–400 mg/dL. With the sensitivity of 0.001 (∆A/(mg/dL)), the biosensor response reaches stability after five minutes, and the limit of detection (LOD) of the TG optical biosensor is 15 mg/dL. Relative standard deviation (RSD) in a reproducibility test was 2.5%, with a 15-day lifespan.

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“…E. coli GldA has been overexpressed for the increased fermentative metabolism of crude glycerol. Recombinant purified GldA protein is also clinically used as a coupling enzyme for lipoprotein lipase-based assays in the quantitation of triglycerides (Mamoru et al, 1977). Its kinetic and biochemical properties have been well characterized (Piattoni et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Structure of glycerol dehydrogenase (GldA) fromEscherichia coli

et al. 2019

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Escherichia coli (strain K‐12, substrain MG1655) glycerol dehydrogenase (GldA) is required to catalyze the first step in fermentative glycerol metabolism. The protein was expressed and purified to homogeneity using a simple combination of heat‐shock and chromatographic methods. The high yield of the protein (∼250 mg per litre of culture) allows large‐scale production for potential industrial applications. Purified GldA exhibited a homogeneous tetrameric state (∼161 kDa) in solution and relatively high thermostability (Tm = 65.6°C). Sitting‐drop sparse‐matrix screens were used for protein crystallization. An optimized condition with ammonium sulfate (2 M) provided crystals suitable for diffraction, and a binary structure containing glycerol in the active site was solved at 2.8 Å resolution. Each GldA monomer consists of nine β‐strands, thirteen α‐helices, two 310‐helices and several loops organized into two domains, the N‐ and C‐terminal domains; the active site is located in a deep cleft between the two domains. The N‐terminal domain contains a classic Rossmann fold for NAD+ binding. The O1 and O2 atoms of glycerol serve as ligands for the tetrahedrally coordinated Zn2+ ion. The orientation of the glycerol within the active site is mainly stabilized by van der Waals and electrostatic interactions with the benzyl ring of Phe245. Computer modeling suggests that the glycerol molecule is sandwiched by the Zn2+ and NAD+ ions. Based on this, the mechanism for the relaxed substrate specificity of this enzyme is also discussed.

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A simple colorimetric method for determination of serum triglycerides with lipoprotein lipase and glycerol dehydrogenase

Cited by 53 publications

References 15 publications

Comparison between Biochemical Analysis of Cattle Amniotic Fluid and Maternal Serum Components during Pregnancy.

Comparison between Biochemical Analysis of Cattle Amniotic Fluid and Maternal Serum Components during Pregnancy.

Construction of a Hydrogel Pectin-Based Triglyceride Optical Biosensor with Immobilized Lipase Enzymes

Structure of glycerol dehydrogenase (GldA) fromEscherichia coli

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