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Peptide Fractions (peptide + fraction)
Selected AbstractsBosentan treatment of portopulmonary hypertension related to liver cirrhosis owing to hepatitis CEUROPEAN JOURNAL OF CLINICAL INVESTIGATION, Issue 2006W. Grander Abstract Pulmonary arterial hypertension (PAH) with coexisting portal hypertension has been defined as portopulmonary hypertension (PPHTN). It is often related to liver cirrhosis of various aetiologies and is associated with a high mortality rate. Endothelin-1 (ET) is supposed to play an important role in the pathogenesis of PAH as well as portal hypertension. Therefore, therapy with an ETA/ETB receptor antagonist might be of use in the treatment of PPHTN. We report the case of a 76-year-old male with liver cirrhosis owing to chronic hepatitis C virus infection and PPHTN who was treated with the dual ETA/ETB receptor antagonist bosentan. The patient showed remarkable improvement of 6-min walking distance from 300 to 480 m after 2 weeks and to 540 m after 14 weeks, respectively. In addition, a significant decline of N-terminal pro B-type natriuretic peptide fraction (NT-proBNP) from 4928 ng mL,1 to 640 ng mL,1 was observed. Bosentan might be a promising new therapeutical option for patients suffering from PPHTN. [source] Angiotensin converting enzyme inhibition of fish protein hydrolysates prepared from alkaline-aided channel catfish protein isolateJOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 12 2007Ann E Theodore Abstract Peptides derived from aquatic animals have been shown to have inhibitory activity against angiotensin converting enzyme (ACE), which is a key enzyme behind elevated blood pressure. In this study a catfish protein isolate was prepared and hydrolyzed to 5%, 15% and 30% degrees of hydrolysis (% DH) and soluble peptides separated from the total hydrolysate. The hydrolysate and its soluble peptide fraction were studied separately. Increased hydrolysis produced smaller peptides, with the smallest peptides remaining in the soluble fraction. Both hydrolysates and its soluble fraction had high ACE inhibition activities, from 70% to 90.6%, depending on fraction and % DH. Results suggested that there is not a simple relationship between average peptide size and extent of % DH and ACE inactivation, but clearly the soluble fraction of the hydrolysate, containing the smallest peptides, is responsible for most of the ACE inhibition activity of the hydrolysate. Hydrolysates prepared from a pure and uniform catfish protein isolate substrate do therefore show a potential for ACE inhibition and may find use as bioactive ingredients. Copyright © 2007 Society of Chemical Industry [source] Anticancer activity of hydrophobic peptides from soy proteinsBIOFACTORS, Issue 1-4 2000Song E Kim Abstract An anticancer peptide from soy protein was purified and isolated. Defatted soy protein was hydrolyzed with thermoase and hydrophobic peptides were extracted with ethanol. The peptide extract was fractionated by XAD-2 hydrophobic, gel filtration chromatography, and different C18 HPLCs. Anticancer activity of each fraction was assayed by measuring in vitro cytotoxicity on P388D1, a mouse monocyte macrophage cell line. IC50 value of a peptide fraction from Sephadex G-25 chromatography was 0.16 mg/ml. This peptide fraction at 1 mg/ml significantly affected cell cycle progression by arresting P388D1 at G2/M phases. Finally purified peptide from analytical C18 HPLC was nonapeptide of which molecular weight was 1157 Da and the sequence was X-Met-Leu-Pro-Ser-Tye-Ser-Pro-Tyr. [source] IN VITRO DIGESTIBILITY OF CHINESE TARTARY BUCKWHEAT PROTEIN FRACTIONS: THE MICROSTRUCTURE AND MOLECULAR WEIGHT DISTRIBUTION OF THEIR HYDROLYSATESJOURNAL OF FOOD BIOCHEMISTRY, Issue 5 2006XIAONA GUO ABSTRACT Our previous study showed that in vitro pepsin digestibility of Chinese tartary buckwheat protein was relatively low compared to those of other edible seeds. In vitro pepsin digestibilities of four protein fractions of tartary buckwheat, microstructure and molecular weight (MW) distributions of hydrolysates were investigated. In vitro pepsin digestion assay showed that the digestibilities of tartary buckwheat protein fractions were albumin (81.20%), globulin (79.56%), prolamin (66.99%) and glutelin (58.09%). Scanning electron microscopy showed that albumin and globulin fractions were digested by pitting from the outer surface to the inner part and were more digestible, while prolamin and glutelin fractions resisted digestion because only the outer surfaces of their protein bodies were digested and the interior was protected. MW distribution of the hydrolysates from the four protein fractions was determined by high-performance liquid chromatography. The hydrolysates of albumin mainly consisted of polypeptides with lower MW. The hydrolysates of glutelin had larger polypeptides together with small and medium-sized peptide fractions. [source] Antioxidant activity of peptide fractions derived from cottonseed protein hydrolysateJOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 11 2010Dandan Gao Abstract BACKGROUND: Cottonseed protein is widely regarded as a potential source of nutrients for humans and animals, but it is mainly used as forage in China. In the present study, Neutrase was employed to hydrolyse cottonseed protein to produce a hydrolysate with antioxidant activity suitable for conversion to high-value products. The antioxidant potential of the cottonseed protein hydrolysate (CPH) and its fractions was investigated using different in vitro methods. Furthermore, the amino acid composition of the CPH fractions was determined to evaluate the relationship between antioxidant activity and amino acid composition. RESULTS: The CPH prepared using Neutrase was separated into four fractions (I, II, III and IV) by gel filtration on Sephadex G-25. All fractions were effective antioxidants, with fraction III (0.8,1.2 kDa) showing the strongest activity. The amino acid analysis showed that fraction III also had the highest total amino acid content (616.8 g kg,1 protein) and was rich in Phe, His, Pro, Met, Ile and Cys compared with the other fractions. CONCLUSION: The results showed that the hydrolysate derived from cottonseed protein, particularly fraction III, could be a natural antioxidant source suitable for use as a food additive. Copyright © 2010 Society of Chemical Industry [source] Plant Protein Hydrolysates: Preparation of Defined Peptide Fractions Promoting Growth and Production in Animal Cells CulturesBIOTECHNOLOGY PROGRESS, Issue 5 2000Franti, ek Fran A new approach was applied with the aim at producing plant protein hydrolysates less heterogeneous and less contaminated with nonpeptide substances than are the presently available digests. A significant reduction of nonprotein contaminants was achieved by extraction of the plant material, soy flour or wheat flour, with acetone prior to isolation of the protein. Enzymes of nonanimal origin, papain or Pronase, were used for protein hydrolysis. The components of the hydrolysates were resolved by low-pressure liquid chromatography. Separation of peptide fractions and of remaining nonpeptide contaminants was achieved using small-pore size-exclusion chromatography matrices, Sephadex G-15 or Biogel P-2. Individual peptide fractions, both from soy protein and from wheat gluten, varied substantially in their growth-promoting and production-enhancing activities when tested on a mouse hybridoma culture in protein-free medium. The highest enhancement of viable cell density in batch cultures was 180% of control, and the highest enhancement of final immunoglobulin concentration was more than 230% of control. The existence of marked differences in activity of individual peptide fractions leads to a suggestion that the hydrolysates may provide peptides exerting specific positive effects on cultured animal cells. [source] In vitro haem solubility of red cell fraction of porcine blood under various treatmentsINTERNATIONAL JOURNAL OF FOOD SCIENCE & TECHNOLOGY, Issue 4 2010Tong-Xun Liu Summary An in vitro peptic digestion at gastric pH 2.0 was used to assess the haem solubility of red cell fraction (RCF) of porcine blood derived samples. The in vitro haem solubility of the RCF decreased greatly in the denaturated form of haemoglobin. However, the native haemoglobin was susceptible to be hydrolysed by enzyme mixture of Flavourzyme and Alcalase. The in vitro digestion of the hydrolysates showed that the highest haem solubility was reached at degree of hydrolysis between 8.75% and 12.33%. The in vitro haem solubility was positively correlated with content of the highly soluble peptides with molecular weights ranged from 7.5 kDa to 1 kDa, but negatively with peptides fractions >7.5 kDa and <1 kDa, mostly due to the precipitation of the highly molecular weight fraction (>7.5 kDa) and part of small peptides (<1 kDa) with higher haem/peptide ratio, which was confirmed by gel filtration chromatograms and by the analysis of the precipitate at pH 2.0. [source] | |||||||||||||