scholarly journals The isolation and partial characterization of ribonuclease A from Bison bison

1973 ◽  
Vol 135 (3) ◽  
pp. 427-441 ◽  
Author(s):  
Gordon R. Stewart ◽  
Kenneth J. Stevenson
Keyword(s):  
Amino Acid ◽  
Amino Acid Content ◽  
Attachment Site ◽  
Iodoacetic Acid ◽  
Exchange Chromatography ◽  
Bison Bison ◽  
Total Amino Acid ◽  
Affinity Column ◽  
Acid Extraction ◽  
Sodium Phosphate Buffer

1. Bison ribonuclease was isolated from pancreas glands of Bison bison by acid extraction, (NH4)2SO4 fractionation, affinity chromatography on Sepharose–5′-(4-aminophenylphosphoryl)uridine 2′,3′-phosphate and ion-exchange chromatography on Bio-Rex-70. 2. The selectivity of the affinity column towards bison ribonuclease in heterogeneous protein solutions was greatly improved by employing piperazine buffers at pH5.3, which decreased non-specific interactions of other proteins. Rapid desorption from the affinity column was obtained with sodium phosphate buffer (pH3). 3. Bison ribonuclease has a total amino acid content very similar to ox ribonuclease. Inactivation of bison ribonuclease with iodoacetic acid leads to the formation of 0.62 residues of π-carboxymethylhistidine and 0.36 residues of τ-carboxymethylhistidine. The amino acid composition of peptides isolated from diagonal peptide ‘maps’ and also of peptides isolated after pH1.6 and 2.4 two-dimensional high-voltage electrophoresis of a digest of bison ribonuclease labelled with pyridoxal 5-phosphate indicates that there is complete homology between ox and bison ribonucleases. 4. The Schiff-base attachment site of pyridoxal 5-phosphate was identified as lysine-41 by NaBH4 reduction followed by peptide isolation.

scholarly journals ISOLASI PROTEIN DAN PRODUKSI KONSENTRAT PROTEIN DAUN (KPD) SEBAGAI SUPLEMEN PAKAN TERNAK

Pastura ◽  
2019 ◽  
Vol 7 (2) ◽  
pp. 88
Author(s):  
Yatno Yatno ◽  
Suparjo Suparjo ◽  
Rasmi Murni
Keyword(s):  
Amino Acid ◽  
Isoelectric Point ◽  
Essential Amino Acid ◽  
Crude Protein ◽  
Amino Acid Content ◽  
Acetate Buffer ◽  
Total Amino Acid ◽  
Acid Extraction ◽  
Randomized Design ◽  
Ph Buffer

The research aim to determine the effect of extraction using various combination of pH alkaline-acid to protein and amino acid content of Lamtoro Protein Concentrate Leaf (LPCL). Completely Randomized Design (CRD) with 3 treatments and 5 replications. The Lamtoro Leaf Meal (LLM) (50 gram) was blended in NaOH (200 ml) for 15 menit and centrifuged to separate the supernatant from extracted LLM. The extracted LLM was re-extracted with buffer acetat pH 4,6 and sentrifuged again to separate supernantant from extracted LLM. Both supernatant from NaOH and buffera acetat pH 4,6 extraction were mixed and precipitated with buffer phospat until isoelectric point. The treatments were tested consisted of extracted with NaOH pH 8, NaOH pH 9 and NaOH pH 10. The parameters measured; isoelectric point at precipited, crude protein, total amino acid (TAA), total essential amino acid (TEAA) and individual amino acid. The results showed that the precipited obtained isoelectric point pH 7 was 2.66; 1.03 and 2.58 gram at the extraction treatments using NaOH at pH 8, 9 and 10, respectively. LPCL extracted using NaOH at pH 9 and 10 contained a high crude protein of 54.82 and 52.60% higher than the extraction using NaOH at pH 8 of 46.98%. The total amount of amino acid and essential amino acid (AAE) of LPCL were highest in treatment using NaOH at pH 10 of 26,58; 13.31 %, respectively. Combination extraction LLM using pH buffer 10 followed by re-extract using acetate buffer pH 4,6 contains crude protein and good essential amino acid, especially leucine. Conclution of the research that the combination extraction using NaOH at pH 10 and followed by re-extract using acetate buffer at pH 4.6 is the best treatment contain crude protein and essential amino acid at LPCL. Keywords : Crude protein, essential amico acid, extraction.

scholarly journals Purification and characterization of a uterine retinol-binding protein in the bitch

1995 ◽  
Vol 311 (2) ◽  
pp. 407-415 ◽  
Author(s):  
W C Buhi ◽  
I M Alvarez ◽  
V M Shille ◽  
M J Thatcher ◽  
J P Harney ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dna Sequences ◽  
Binding Protein ◽  
Amino Acid Content ◽  
Amino Acid Sequences ◽  
Retinol Binding Protein ◽  
Total Amino Acid ◽  
Major Protein ◽  
Serum Retinol ◽  
Two Dimensional Gel Electrophoresis

A major canine endometrial secreted protein (cP6, 23,000-M(r)) was purified by ion-exchange and gel-filtration chromatography and characterized by two-dimensional gel electrophoresis. Anti-[human retinol-binding protein (hRBP)] serum identified cP6 on immunoblot analysis and immunoprecipitated cP6 from culture medium. This major protein was also shown to bind [3H]retinol. N-terminal and internal amino acid sequences were determined and compared with previously identified protein, RNA, or DNA sequences. N-terminal analysis revealed that cP6 had high identity and similarity to serum retinol-binding proteins (RBPs), while internal sequence analysis showed a strong similarity to rat androgen-dependent epididymal protein and beta-lactoglobulins. Amino acid analysis, however, showed significant differences between these proteins and cP6 in both total amino acid content and certain selected amino acids. Immunohistochemical analysis showed staining for RBP only in the uterine luminal epithelium. These studies suggest that bitch endometrium secretes a family of proteins (cP6), some of which bind [3H]retinol, are immunologically related to the RBP family, and have N-terminal and internal sequences with a high similarity to RBP, beta-lactoglobulins and other members of the lipocalin family. This family of proteins may be important in early development for supplying retinol or derivatives to the developing embryo.

Comparison of Three Methods for Calculating Protein Content in Developing Apple Flower Buds

1992 ◽  
Vol 75 (4) ◽  
pp. 734-737 ◽  
Author(s):  
Shahrokh Khanizadeh ◽  
Deborah Buszard ◽  
Constantinos G Zarkadas
Keyword(s):  
Amino Acid ◽  
Protein Content ◽  
Conversion Factor ◽  
Amino Acid Content ◽  
Good Method ◽  
Accurate Method ◽  
Total Amino Acid ◽  
Total Protein Content ◽  
Flower Buds ◽  
Flower Bud

Abstract Three methods (Kjeldahl, sulfuric acid-hydrogen peroxide, and summation of amino acid content) for determining and calculating the protein content of apple flower buds were compared. Quantitation of protein content based on summation of amino acids appears to be the most accurate method. A new nitrogen:protein conversion factor (5.51) was calculated based on total amino acid analysis. This new conversion factor could replace the conventional 6.25 factor for estimating total protein content of apple flower bud by the Kjeldahl method. However, Kjeldahl is not an accurate method for estimating protein content in apple flower bud tissue, regardless of the conversion factor, and probably would not be a good method for estimation of protein in other plant species.

scholarly journals AMINO ACID PROFILE OF A BASIDIOMYCETOUS EDIBLE MUSHROOM-LENTINUS SAJOR-CAJU

2017 ◽  
Vol 9 (9) ◽  
pp. 252
Author(s):  
Lata . ◽  
Narender Singh Atri
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Content ◽  
Standard Technique ◽  
Edible Mushroom ◽  
Amino Acid Profile ◽  
Total Amino Acid ◽  
Isoleucine Leucine ◽  
Total Amino Acid Content ◽  
Basidiomycetous Mushroom

Objective: In this paper amino acid profile of Lentinus sajor-caju (Fr.) Fr., a basidiomycetous mushroom has been investigated.Methods: During the evaluation 15 amino acids (lysine, aspartic acid, serine, threonine, glutamic acid, cysteine, glycine, alanine, valine, methionine, isoleucine, leucine, tyrosine, phenylalanine and histidine) were determined from the dried sample of Lentinus sajor-caju by following the standard technique of biochemistry using ion-exchange chromatography.Results: The total amino acid content has been evaluated at 18.82 g/100g. Amongst the evaluated amino acids, exogenous amino acid lysine (6.66 g/100g) is preponderantly present in comparison to all other amino acids. The essential amino acid (EAA) index (44.64%) and biological value (BV=36.93%) has also been determined for the examined sample.Conclusion: Lentinus sajor-caju (Fr.) Fr. is a potential source of quality protein with a substantial proportion of exogenous and endogenous amino acids.

scholarly journals Preparation of Selenium-Enriched Yeast by Re-Using Discarded Saccharomyces cerevisiae from the Beer Industry for Se-Supplemented Fodder Applications

2019 ◽  
Vol 9 (18) ◽  
pp. 3777 ◽  
Author(s):  
Wu ◽  
Liu ◽  
Sun ◽  
Lin ◽  
Zhan ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Acid Content ◽  
Lethal Dose ◽  
Amino Acid Content ◽  
Total Amino Acid ◽  
Toxic Level ◽  
Organic Selenium ◽  
Removal Capacity ◽  
Beer Industry

Both inorganic and organic selenium (Se) can prevent and treat various diseases caused by Se deficiency. However, organic Se has less toxicity and a higher absorption rate than inorganic Se. In this study, inorganic Se (Na2SeO3) was bio-transformed into Se-enriched discarded beer yeast (Se-enriched DB-yeast) through fermentation accumulation by re-using discarded Saccharomyces cerevisiae from the beer industry for Se-enriched fodder application. Through a single-factor experiment and L9(34)-orthogonal test for optimization of fermentation conditions, the Se content and biomass of Se-enriched DB-yeast were calculated as 14.95 mg/L and 7.3 g/L, respectively, under the optimized condition. The total amino-acid content of Se-enriched DB-yeast was increased by 9.9% compared with that from DB yeast. Additionally, alkaline amino-acid content was increased, whereas acidic amino-acid and sulfur-containing amino-acid contents were decreased. Reducing capacity, hydroxyl radical removal capacity, and sulfhydryl content after treatment with H2O2 of the Se-enriched DB-yeast extracted protein were obviously increased compared with those of the DB-yeast extracted protein. Mouse and genetically improved farmed tilapia (Oreochromis niloticus) (GIFT) bioassays showed that the Se sedimentation of organs and serum indexes after feeding Se-enriched DB-yeast-containing fodder were higher than those of DB-yeast-containing fodder. The half lethal dose (LD50) of Se-enriched DB-yeast (9260.0 mg/kg body weight (BW), 18.97 mg/kg of Se content, non-toxic level) was considerably higher than that of Na2SeO3 (20.0 mg/kg BW, 5.08 mg/kg of Se content, highly toxic level) against mouse. Therefore, Se-enriched yeast prepared by re-using discarded S. cerevisiae from beer industry fermentation accumulation has the potential to be a safe and effective Se-enriched fodder additive.

Variations in total amino acid content of peanut meal

1973 ◽  
Vol 50 (12) ◽  
pp. 521-523 ◽  
Author(s):  
C. T. Young ◽  
G. R. Waller ◽  
R. O. Hammons
Keyword(s):  
Amino Acid ◽  
Acid Content ◽  
Amino Acid Content ◽  
Peanut Meal ◽  
Total Amino Acid ◽  
Total Amino Acid Content
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