For biochemical analysis, serum aliquots were obtained by placing the blood samples in serum tubes at a temperature of 24 °C for approximately 30 min. After clotting, the blood tubes were centrifuged at 3000 rpm for 10 min using a Himac CR 21 G centrifuge (Hitachi, Tokyo, Japan). Supernatants were removed and stored at −20 °C for further analysis. Serum chemistry was assessed using a Synchron CX4 Clinical System (Beckman Coulter, Brea, CA USA) according to the manufacturer’s protocol (Beijing Leadman Biochemistry Technology Co. Ltd, Beijing, China). The serum activities of ALB, ALP, ALT and AST were used as biochemical markers of hepatic damage.
Himac cr 21 g
Manufactured by Hitachi
Sourced in Japan
The Himac CR 21 G is a high-performance centrifuge designed for laboratory applications. It features a maximum speed of 21,000 rpm and a maximum relative centrifugal force (RCF) of 52,600 xg. The centrifuge has a compact design and can accommodate a variety of rotor types to suit different sample sizes and requirements.
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Lab products found in correlation
4 protocols using himac cr 21 g
1
Serum Biochemistry Analysis Protocol
2
Comprehensive Toxicology Evaluation Protocol
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The number of sacrificed mice was 10 per group (5 mice/sex) at weeks 26 and 52. The remaining survival mice were sacrificed at the final scheduled necropsy (78 weeks). According to the OECD and FDA Redbook guidelines, standard hematology and serum chemistry parameters should be evaluated at weeks 26, 52, and 78. Following an overnight fast, animals were anesthetized and euthanized, and then, the blood samples were collected from each mice for hematology and serum biochemistry. K+ EDTA was used as an anticoagulant in blood for the hematology tests. For clinical chemistry, blood samples were placed in serum tubes at room temperature for approximately 30 min to obtain serum aliquots. After clotting, the blood tubes were centrifuged at 3000 rpm for 10 min by using Himac CR 21 G centrifuge (Hitachi, Tokyo, Japan). The supernatants were decanted and stored at -20°C for further serum biochemistry analysis.
3
Purification and Characterization of FELP
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P. aibuhitensis was provided by Yancheng Fengyueyuan Fishing Bait Co., Ltd. (Huangshagang, China). The isolation of FELP from P. aibuhitensis was based on the method of Zhihui Deng et al. (2010) with modifications [35 (link)]. All operations were carried out at 4 °C. For specific operating procedures, refer to Ge et al. (2022) [40 (link)]. The 500 mg dried sample was immersed in 100 mL PBS for 3 h and centrifuged at 9900× g for 20 min at 4 °C using a Himac CR 21G high-speed floor centrifuge (Hitachi, Tokyo, Japan). Ammonium sulfate was stirred into the supernatant until dissolved, reaching 30 to 90% saturation, and then left for 2 h. The precipitates collected with centrifugation at 15,400× g for 30 min were resuspended in PBS (pH 7.4) and dialyzed using dialysis membranes (MWCO: 10 kDa) against 0.02 M Tris-HCl (pH 7.4) for 48 to 72 h. The dialyzed sample was pre-cooled at −80 °C for 4 h and lyophilized using a freeze-dryer (Labconco Freezone 2.5 L, Kansas City, MO, USA). The fibrinolytic activity and protein content of the samples taken at each ammonium sulphate saturation level were measured to calculate the specific activity.
4
Tissue Fractionation and Biochemical Analysis
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Heparinized blood samples were centrifuged at 2150× g for 20 min at 4 °C. Samples of plasma supernatant were collected for biochemical analyses. Plasma CK and AST were measured using assay kits according to the manufacturer’s instructions. Sorbitol dehydrogenase (SDH) activities were measured as previously described [12 (link)].
Excised myocardial ventricular tissue samples were rinsed with ice-cold homogenizing buffer (50 mM Tris-HCl, 325 mM sucrose and 1 mM EDTA, pH 7.0). Liver tissue samples were rinsed with ice-cold homogenizing buffer (5 mM Tris-HCl, 250 mM sucrose and 0.1 mM EDTA, pH 7.0). Tissue homogenates were prepared by homogenizing ~0.5 g of minced tissue in 5 mL ice-cold homogenizing buffer (i.e., a 10% homogenate (w/v)) in a Teflon-in glass homogenizer (Glas-Col, Terre Haute, IN, USA) on ice at a speed of 40 rpm for 10 strokes. The homogenates were centrifuged (Himac CF 9RX, Hitachi Koki Co., Ltd., Ibaraki, Japan) at 600× g for 20 min at 4 °C. Mitochondrial fractions were obtained by centrifugation (Himac CR21G, Hitachi Koki Co., Ltd., Ibaraki, Japan) at 9200× g for 30 min at 4 °C.
Excised myocardial ventricular tissue samples were rinsed with ice-cold homogenizing buffer (50 mM Tris-HCl, 325 mM sucrose and 1 mM EDTA, pH 7.0). Liver tissue samples were rinsed with ice-cold homogenizing buffer (5 mM Tris-HCl, 250 mM sucrose and 0.1 mM EDTA, pH 7.0). Tissue homogenates were prepared by homogenizing ~0.5 g of minced tissue in 5 mL ice-cold homogenizing buffer (i.e., a 10% homogenate (w/v)) in a Teflon-in glass homogenizer (Glas-Col, Terre Haute, IN, USA) on ice at a speed of 40 rpm for 10 strokes. The homogenates were centrifuged (Himac CF 9RX, Hitachi Koki Co., Ltd., Ibaraki, Japan) at 600× g for 20 min at 4 °C. Mitochondrial fractions were obtained by centrifugation (Himac CR21G, Hitachi Koki Co., Ltd., Ibaraki, Japan) at 9200× g for 30 min at 4 °C.
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