L 8800 automatic amino acid analyzer

Manufactured by Hitachi

Sourced in Japan

The L-8800 automatic amino acid analyzer is a laboratory instrument designed for the analysis and quantification of amino acids. It utilizes ion exchange chromatography and post-column derivatization techniques to separate and detect amino acids in various sample types. The core function of the L-8800 is to provide accurate and reliable amino acid analysis for researchers and laboratories.

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Lab products found in correlation

L 8800 aa analyzer, by Hitachi (1 mentions) Ankom200 fibre analyzer, by ANKOM Technology (1 mentions)

Close spelling variants of this product

L-8800 (123 citations) Automatic analyzer (51 citations) Amino Acid Analyzer (25 citations)

11 protocols using l 8800 automatic amino acid analyzer

Amino Acid Profiling of Clam Hydrolysates

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The frozen portions of the clams were hydrolyzed for 22 h at 110 ± 1 °C with 6 M HCl in sealed glass tubes filled with nitrogen. Following hydrolysis, 1 mL of hydrolyzate was withdrawn and evaporated to dryness under vacuum at 45 °C to remove HCl. The hydrolyzate was dissolved in 1 mL of sodium citrate buffer (pH 2.2), and then the samples were analyzed by a Hitachi L8800 Automatic Amino Acid Analyzer (Hitachi, Tokyo, Japan). The identity and quantity of each amino acid was assessed by comparison with the retention time and peak area of a standard (Sigma).
The tryptophan content was determined in a separate analysis. The weighed samples were hydrolyzed in 5 N NaOH containing 5% SnCl2 (w/v) for 20 h at 110 °C (Hugli and Moore 1972 (link)). After hydrolysis, the hydrolyzate was neutralized with 6 N HCl and centrifuged, and then the supernatant was analyzed by a Hitachi L8800 Automatic Amino Acid Analyzer. The identity and quantity of tryptophan was assessed by comparison with the retention time and peak area of a standard (Sigma). All determinations were performed in triplicate. Amino acid ((threonine (Thr), tryptophan (Trp), cysteine + methionine (Cys + Met), valine (Val), phenylalanine + tryptophan (Phe + Tyr), isoleucine (Ile), leucine (Leu), and lysine (Lys)) contents were expressed as mg/g wet weight.

Tabakaeva O.V., Tabakaev A.V, & Piekoszewski W. (2018). Nutritional composition and total collagen content of two commercially important edible bivalve molluscs from the Sea of Japan coast. Journal of Food Science and Technology, 55(12), 4877-4886.

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Amino Acid Determination in Diets and Plasma

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The diets were analyzed for CP (N × 6.25) according to AOAC [24 ]. Amino acids except methionine, cystine, and tryptophan, were determined using Ion-Exchange Chromatography by a Hitachi L-8800 AA Analyzer (Tokyo, Japan) after acid hydrolysis with 6 N HCl (reflux for 24 h at 110°C). Cystine was determined as cysteic acid and methionine as methionine sulphone after peroxidation with performic acid and pre-column derivation using phenylisothiocyanate (L-8800 Hitachi Automatic Amino Acid Analyzer, Tokyo, Japan). Tryptophan was determined after hydrolyzing with 4 M NaOH at 110°C for 20 h using phenylisothiocyanate (Model 76337, Agilent Technologics, Waldbronn, Germany).
Plasma AA concentrations were determined by Ion-Exchange Chromatography with physiological fluid analysis conditions (S-433D AA Analyzer, Sykam, Germany) as described by Boucher, Charret, Coudray-Lucas, Giboudeau and Cynober [25 (link)]. SUN concentration was determined by a Biochemical Analytical Kit (C013-1, NJJC, Nanjing, China) according to the instructions provided by the manufacturer. Concentrations of PAH in plasma were measured as described by Harvey and Brothers [26 (link)].

Qiu K., Qin C.F., Luo M., Zhang X., Sun W.J., Jiao N., Li D.F, & Yin J.D. (2016). Protein Restriction with Amino Acid-Balanced Diets Shrinks Circulating Pool Size of Amino Acid by Decreasing Expression of Specific Transporters in the Small Intestine. PLoS ONE, 11(9), e0162475.

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Amino Acid Composition Analysis

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Amino acid composition was determined using the method described by Lu et al. (2008) . The wet muscle samples were cut into slices and dried in a vacuum-freeze dryer, allowed to equilibrate with atmospheric moisture for 24 h, and then finely ground to pass a 60-mesh sieve. The amino acid composition of the muscle powder was analyzed using ionexchange chromatography with an automatic amino acid analyzer (L-8800 Hitachi Automatic Amino Acid Analyzer, Tokyo, Japan) after hydrolysis with 6 N HCl at 110°C for 24 h. Methionine, cystine and tryptophan were partly destroyed under acid hydrolysis. Tryptophan was determined after alkaline hydrolysis with 4 N NaOH for 22 h at 110°C. Methionine and cystine were analyzed after cold formic acid oxidation for 16 h before acid hydrolysis. Duplicate analyses were performed on all samples.

Zhang S.H., Shen L.Y., Luo J., Wu Z.H., Jiang Y.Z., Tang G.Q., Li M.Z., Bai L., Li X.W, & Zhu L. (2015). Analysis of carcass and meat quality traits and nutritional values of hybrid wild boars under different crossing systems. Genetics and molecular research : GMR, 14(1).

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Muscle Composition Analysis

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About 50 g of breast or leg muscle samples were freeze-dried for 72 h to calculate the percentage of dry matter. Dried samples were crushed and analyzed for crude protein and fat content according to AOAC (1995) methods. The amino acid content in muscle was analyzed on an L-8800 automatic amino acid analyzer (Hitachi, Japan).

Yu Q., Fang C., Ma Y., He S., Ajuwon K.M, & He J. (2020). Dietary resveratrol supplement improves carcass traits and meat quality of Pekin ducks. Poultry Science, 100(3), 100802.

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Detailed Feed Composition Analysis

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Feed samples were collected every two days, and composite samples of the feedstuffs were prepared biweekly. The samples were dried in a forced-air oven at 55 °C for 48 h to determine the dry matter (DM); the samples were subsequently ground (Wiley Mill, Thomas Co.; Philadelphia, PA, USA) to pass through a 1 mm sieve and then stored at room temperature until analysis. The analyses included the determination of DM (method 934.01), N (Leco TruMac CN, St. Joseph, MI, USA; method 990.03), ash (method 930.15), calcium (method 96.08) and phosphorous (method 946.06) contents according to AOAC methods [22 ]. In addition, neutral detergent fibre (NDF) and acid detergent fibre (ADF) were analysed using an ANKOM200 Fibre Analyzer (ANKOM Technology Corp., Macedon, NY, USA) using the filter bag technique, which involved the addition of heat-stable α-amylase and sodium sulphite [23 (link)]. Following hydrolysis with 6 N HCl at 110 °C for 24 h, the AAs in the diet were assayed through ion-exchange chromatography using an automatic AA analyser (Hitachi L8800 Automatic Amino Acid Analyzer; Tokyo, Japan).

Wang W., Ye L., Dou X., Liu H, & Han D. (2023). Effects of Rumen-Protected Methionine Supplementation on Growth Performance, Nutrient Digestion, Nitrogen Utilisation and Plasma Amino Acid Profiles of Liaoning Cashmere Goats. Animals : an Open Access Journal from MDPI, 13(19), 2995.

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Amino Acid Composition Analysis of Dried Leaves

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Powdered dried leaves (0.1 g) were transferred into a 20-ml hydrolysis tube with 10 ml of 6 mol l⁻¹ hydrochloric acid. The hydrolysis tube was sealed under vacuum and transferred to a constant-temperature drier at 110 ± 2°C for 22 h. After the tubes were removed from the dryer and cooled, the hydrolysis liquid was filtered, transferred into a 50-ml volumetric flask, and diluted with deionized water to scale. Then, 1 ml of the diluted hydrolysis liquid was withdrawn and dried in a vacuum drier at 40–50°C. The residue was dissolved in 1 ml of sodium citrate-hydrochloric acid buffer solution (pH 2.2) for analysis. The concentration and composition of amino acids were determined by an L-8800 automatic amino acid analyzer (Hitachi, Tokyo, Japan).

Zhang Y., Feng L., Jiang H., Zhang Y, & Zhang S. (2017). Different Proteome Profiles between Male and Female Populus cathayana Exposed to UV-B Radiation. Frontiers in Plant Science, 8, 320.

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Nutritional Composition of ATC

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The contents of ergosterol, cordycepin, and cordycepic acid, and Cordyceps polysaccharide in ATC were determined by high-performance liquid chromatography (15 (link)). The amino acid content was determined using a HITACHI L-8800 automatic amino acid analyzer (HITACHI Co., Tokyo, Japan). The DM (method 930.15), CF (method 993.21), crude ash (method 942.05), EE (method 920.39), and CP (method 976.05) were analyzed according to the methods of the Association of Official Analytical Chemists (16 ).

Li Y., Jiang X., Xu H., Lv J., Zhang G., Dou X., Zhang Y, & Li X. (2020). Acremonium terricola culture plays anti-inflammatory and antioxidant roles by modulating MAPK signaling pathways in rats with lipopolysaccharide-induced mastitis. Food & Nutrition Research, 64, 10.29219/fnr.v64.3649.

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Amino Acid Profiling in Goat Tissues

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After goat slaughter, the jejunal and ileal mucosa, and longissimus dorsi were immediately separated, and washed with precooled PBS (0.85% NaCl, 1.4 mM KH₂PO₄, 8 mM Na₂HPO₄, pH 7.4), and quickly put into liquid nitrogen and stored at −20°C until analysis. Amino acids in the intestinal mucosa and longissimus dorsi were determined as described elsewhere (Zhang et al., 2013 (link)). An L‐8800 automatic amino acid analyzer (Hitachi) was used to determine the hydrolyzed amino acid content of the jejunal, ileal mucosa, and longissimus dorsi.

Lv X., Chen L., Zhou C., Guo Y., Zhang G., Kang J., Tan Z., Tang S, & Liu Z. (2022). Dietary tea tree (Melaleuca alternifolia) oil supplementation enhances the expressions of amino acid transporters in goat ileal mucosa and improves intestinal immunity. Food Science & Nutrition, 10(11), 3749-3758.

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Plasma amino acid analysis protocol

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Blood samples were obtained on the tenth day of the experiment. The samples were drawn by jugular venipuncture in the morning before feeding and placed into 10 mL heparinized tubes. The plasma was harvested via centrifugation at 3000× g and 4 °C for 20 min. A portion of the plasma was stored at −20 °C until the analysis for urea N content [24 (link)]. A 2 mL sample was placed into a tube containing an equal volume of 5% yellow salicylic acid to precipitate the proteins; subsequently, the samples were centrifuged at 14,000× g and 4 °C for 30 min. Then, the supernatant was obtained to determine the plasma-free AA concentrations using an automatic AA analyser (Hitachi L8800 Automatic Amino Acid Analyzer, Tokyo, Japan).

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Pretreatment and Analysis of Free Amino Acids

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The method from Wang (Wang et al., 2012) was used for pretreatment of FAAs. 2 g sample was fully homogenized with 15 ml trichloroacetic acid solution (15% by mass), and left for 2 hr, then centrifuged at 10,000 × g for 15 min and filtrated. 5 ml of supernatant was taken to adjust pH to 2.0 (with 3 M NaOH), then diluted to 50 ml (with high‐purity water), and filtered through 0.22 μm aqueous phase membranes. All operations were conducted below 4°C. Determination and analysis of FAAs were performed by L‐8800 automatic amino acid analyzer (Hitachi). All analyses were done in triplicate. The identification and quantification were conducted using the retention times and peak area ratios of each FAA standard and the sample, respectively (each of 17 FAA standards in one solution).

Qin J., Wang Z., Wang X, & Shi W. (2020). Effects of microwave time on quality of grass carp fillets processed through microwave combined with hot‐air drying. Food Science & Nutrition, 8(8), 4159-4171.

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