• Journal of Life Science
• /
• v.14 no.6 s.67
• /
• pp.931-937
• /
• 2004

The present investigation was carried out to determine the qualitative difference between 4 varieties of perilla leaves cultivated Miryang area, particularly focusing on the amino acid composition and flavor compounds. Aspartic acid, glutamic acid, glycine, alanine, arginine, and threonine were the major amino acids, and tyrosine and cysteine and methionine containing sulfur were detected as little amount in protein of all perilla leaves. All perilla leaves contained about 34 kinds of free amino acids, and the major free amino acids were same as the protein bound amino acids. However, no significant difference among 4 varieties of perilla leaves was observed in the profiles of protein bound and free amino acids composition. Flavor compounds analyzed by GC-MSD following to extraction of flavor by SDE (Simultaneous Steam Distillation-Extraction) were detected as 51 kinds from 'Leafy perilla 1', 47 kinds from 'Yupsil perilla', 46 kinds from 'Miryang 9' and 'YCPL. The major volatile compound was perilla ketone, its concentration was $145.75\;{\mu}g/g$ in 'Miryang 9', $187.00\;{\mu}g/g$ in 'YCPL', $301.59\;{\mu}g/g$ in 'Leafy perilla l' and $551.42\;{\mu}g/g$ in 'Yupsil perilla', but the other flavor compounds, 3-hexen-l-ol, trans-2-hexenal, $\beta-caryophyllene,\;\alpha-farnesene$ and etc, were less than $20\;{\mu}g/g$.

• Asian-Australasian Journal of Animal Sciences
• /
• v.11 no.6
• /
• pp.725-731
• /
• 1998

Nine crossbred female pigs fitted with the bladder catheters were used to investigate the effects of dietary protein form on the efficiency of absorbed nitrogen for nitrogen retention in growing pigs. Combinations of the main protein sources were corn-soybean meal (CSM; slow + slow absorption rate form), corn-hydrolyzed casein (CAS; slow + rapid absorption rate form) and corn-porcine plasma (CPL; slow + intermediate absorption rate form). All experimental diets were formulated to be isonitrogenous (CP 11%) and isocaloric (3.5 Mcal/kg) and synthetic amino acids were added to the diet as required to maintain an equivalent amino acid profile among diets. Fecal digestibility of nitrogen was not different among treatments (p > 0.10). Ingested nitrogen was absorbed with an apparent efficiency of 82% to 84%. Mean nitrogen retention in pigs fed the CSM diet was as high as for pigs fed the CPL diet (0.74 g N/kg $BW^{0.75}$ per d), which was higher than the N retention rate in pigs fed CAS diet (0.68 g/kg $BW^{0.75}$ per d; P < 0.05). Apparent biological values (ABV = 100 ${\times}$ N retention/absorbed nitrogen) were 63.3%, 58.0% and 61.6% for CSM, CAS, and CPL groups, respectively (p < 0.05). There was no difference in mean energy digestibility among treatments. The efficiency of absorbed lysine utilization was significantly different among treatments (p < 0.05). Pigs fed the CAS diet were inferior to counterparts on the other diets in utilizing absorbed lysine. The ratios of free (and small peptide-bound) to protein-bound amino acids in CSM diet differed considerably from the CAS diet. This may affect the efficiency of amino acids utilization for nitrogen retention if hydrolyzed and intact amino acid pools reach the blood at different times.

• Archives of Pharmacal Research
• /
• v.10 no.3
• /
• pp.193-196
• /
• 1987

Protein methylation occurs ubiquitously in nature and involves N-methylation of lysine, arginine, histidine, alanine, proline and glutamine, O-methylesterfication o dicarboxylic acids, and S-methylation of cysteine and methionine. In nature, methylated amino acids accur in highly specialized proteins such as histones, flagella proteins, myosin, actin, ribosomal proteins. hn RNA-bound protein, HMG-1 and HMG-2 protein, opsin, EF-Tu, EF-$1\alpha$, porcine heart citrate synthase, calmodulin, ferredoxin, $1\alpha$-amylase, heat shock protein, scleroderma antigen, nucleolar protein C23 and IF-3l.

• Journal of Microbiology and Biotechnology
• /
• v.25 no.4
• /
• pp.503-510
• /
• 2015

The iLOV protein belongs to a family of blue-light photoreceptor proteins containing a light-oxygen-voltage sensing domain with a noncovalently bound flavin mononucleotide (FMN) as its chromophore. Owing to advantages such as its small size, oxygen-independent nature, and pH stability, iLOV is an ideal candidate over other reporter fluorescent proteins such as GFP and DsRed. Here, for the first time, we describe the feasibility of applying LOV domain-based fluorescent iLOV as a metal sensor by measuring the fluorescence quenching of a protein with respect to the concentration of metal ions. In the present study, we demonstrated the inherent copper sensing property of the iLOV protein and identified the possible amino acids responsible for metal binding. The fluorescence quenching upon exposure to Cu²⁺ was highly sensitive and exhibited reversibility upon the addition of the metal chelator EDTA. The copper binding constant was found to be 4.72 ± 0.84 µM. In addition, Cu²⁺-bound iLOV showed high fluorescence quenching at near physiological pH. Further computational analysis yielded a better insight into understanding the possible amino acids responsible for Cu²⁺ binding with the iLOV protein.

• BMB Reports
• /
• v.40 no.2
• /
• pp.218-225
• /
• 2007

In Arabidopsis thaliana, the microtubule-associated protein AtMAP65-1 shows various functions on microtubule dynamics and organizations. However, it is still an open question about whether AtMAP65-1 binds to tubulin dimers and how it regulates microtubule dynamics. In present study, the tubulin-binding activity of AtMAP65-1 was investigated. Pull-down and co-sedimentation exp eriments demonstrated that AtMAP65-1 bound to tubulin dimers,at a molar ratio of 1 : 1. Cross-linking experiments showed that AtMAP65-1 bound to tubulin dimers by interacting with $\alpha$-tubulin of the tubulin heterodimer. Interfering the bundling effect of AtMAP65-1 by addition of salt and monitoring the tubulin assembly, the experiment results indicated that AtMAP65-1 promoted tubulin assembly by interacting with tubulin dimers. In addition, five truncated versions of AtMAP65-1, namely AtMAP65-1 $\Delta$N339 (amino acids 340-587); AtMAP65-1 $\Delta$N494 (amino acids 495-587); AtMAP65-1 340-494 (amino acids 340-494); AtMAP65-1 $\Delta$C495 (amino acids 1-494) and AtMAP65-1 $\Delta$C340 (amino acids 1-339), were tested for their binding activities and roles in tubulin polymerization in vitro. Four (AtMAP65-1 $\Delta$N339, $\Delta$N494, AtMAP65-1 340-494 and $\Delta$C495) from the five truncated proteins were able to co-sediment with microtubules, and three (AtMAP65-1 $\Delta$N339, $\Delta$N494 and AtMAP65-1 340-494) of them could bind to tubulin dimers in vitro. Among the three truncated proteins, AtMAP65-1 $\Delta$N339 showed the greatest activity to promote tubulin polymerization, AtMAP65-1 $\Delta$N494 exhibited almost the same activity as the full length protein in promoting tubulin assembly, and AtMAP65-1 340-494 had minor activity to promote tubulin assembly. On the contrast, AtMAP65-1 $\Delta$C495, which bound to microtubules but not to tubulin dimers, did not affect tubulin assembly. Our study suggested that AtMAP65-1 might promote tubulin assembly by binding to tubulin dimers in vivo.

• The Korean Journal of Mycology
• /
• v.11 no.2
• /
• pp.69-77
• /
• 1983

To find antitumor components with low toxicity in the Basidiomycetes of Korea, the carpophores of Flammulina velutipes (Fr.) Singer were extracted with hot water for eight hours. The extract was purified by dialyzing through Visking tube and a protein-bound polysaccharide fraction was obtained as pale brownish amorphous powder after freeze-drying. The fraction was examined for antitumor activity against sarcoma 180 implanted subcutaneously in the left groin in ICR mice. The inhibition ratio of this fraction against the tumor was 62.3% at the dose of 10mg/kg/day for the period of ten days. The tumors in three of the ten treated mice were completely regressed. The chemical analysis of the antitumor component by anthrone and Lowry-Folin methods showed that it consisted of a polysaccharide (42.4%) and a protein (24.5%). The hydrolysis of the polysaccharide moiety with 3% HCl-MeOH and trimethysilylation of the hydrolyzate yielded five monosaccharides which were identified by G.L.C. Several amino acids were identified by an amino acid autoanalyzer in the acid hydrolyzate of the protein moiety.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.24 no.5
• /
• pp.816-828
• /
• 1995

During the industrial preparation and the storage of foods, the side chain of some protein-bound amino acids can react chemically each other or with other molecules present in the food. The following reactions have been described : destruction of amino acids, racemization, protein-protein interactions, reactions of proteins with reducing sugars, oxidizing agents, or polyphenols. Apart from total destruction, the main reacitons are the forming of Maillard reactions products(e.g. fructoselysine) and the crosslinking with other amino acids in the same or in another protein molecule(e.g. lysinoalanine). The most often involved amino acid is lysine because of its free functional ${\varepsilon}-amino$ acid group. Generally derivatives of amino acids or crosslinks in polypeptides influence the bioavailability and the overall digestibility of the protein. This work reviews the technological, analytical, nutritional, and physiological problems related to the formation of fructoselysine and lysinolalnine in human foods, and evaluates the possible health risk for humans. A summary of the available information is of help in considering whether or not the presence of fructoselysine/lysinoalanine in foods represents a danger to man. The reduction in protein quality through these reactions is not a problem for the general population, but it is extremely important in infant foods, since infants are often nourished with a limited number of food product(e.g. formular foods) which are sensitive to the Mailard reaction.

• Asian-Australasian Journal of Animal Sciences
• /
• v.17 no.9
• /
• pp.1277-1280
• /
• 2004

The effect of duodenal infusion with feed oligo-peptide solution on portal absorption of amino acids was investigated in poultry under unanaesthetized conditions. Four peptide solutions were used in the experiment: enzymatic hydrolysates from fish meal, soybean meal, cottonseed meal and rapeseed meal proteins with average molecular weights less than 3,000 Da and 1,000 Da, respectively. Intestinal absorptions of these oligo-peptide solutions were compared by determining the concentration of free amino acid (FAA) in portal blood after the duodenal administrations of oligo-peptide solutions. Absorptive intensity and balance were used to estimate the intestinal absorption rate of amino acids. The absorptive intensities of amino acids were highest for the fish and soybean meal oligo-peptides. The ratios of amino acids absorbed in the portal blood from fish and soybean meal oligo-peptides were more similar to the composition of the infused amino acids than that observed from the cottonseed and rapeseed meal oligo-peptides. A positive correlation was found between absorption rate and proportion of PAA in the oligo-peptides. The higher absorption rate could be contributed to the higher proportion of peptide bound amino acids (PAA). The results suggest that fish and soybean meal protein are significantly more easily hydrolyzed into oligo-peptides (p<0.05) in the gastrointestinal tracts of poultry and as such can be utilized more effectively by body tissues.

• The Korean Journal of Mycology
• /
• v.8 no.1
• /
• pp.13-19
• /
• 1980

To investigate constituents of Russula pseudodelica Lange and Microporus affinis(Blume et Nees) Kuntze, quantitative analyses of free and total amino acids were carried out with G. L.C. and an amino acid autoanalyzer. Polysaccharides of the two mushrooms were extracted with hot water and the filtrate was concentrated. The addition of three volumes of ethanol to the concentrate formed precipitation of crude polysaccharides which were analyzed by G.L.C. and H.P.L.C. Sixteen amino acids and four monosaccharides were identified in the protein-bound poly­saccharides of the two mushrooms. The polysaccharides of M. affinis showed antineoplastic activity against sarcoma 180 implanted in mice.

• The Korean Journal of Mycology
• /
• v.9 no.2
• /
• pp.49-66
• /
• 1981

The objectives of this investigation were to produce artificially an antitumor constituent by submerged culture of the mycelium of Coriolus versicolor (Fr.) Quel., to characterize the influence of various modifications of the nutrient and culture conditions with respect to the pro­duction, to determine chemical composition of the antitumor constituent, and to examine effects of the constituent on the immune response of mice. Submerged agitation of the mycelium in flasks containing a nutrient solution showed its adequate growth. Especially the mycelial growth in the medium containing glucose and yeast extract was abundant. The addition of cotton seed flour or ginseng waste to the medium increased the yield of mycelial growth and the production of the antitumor constituent. The replacement of glucose with starch also yielded the adequate growth. The antitumor constituent extracted from the mycelium and isolated from the culture filtrate was a protein-bound polysaccharide. The analyses of this constituent by GLC and amino acid autoanalysis showed that it contained four monosaccharides and fifteen amino acids. The protein-free polysaccharide of the constituent was also found to exert greater antitumor activity against sarcoma-180 in mice than the entire constituent. The antitumor constituent was found to potentiate the immune response of mice against sheep red blood cell. The protein-bound polysaccharide exerted more favorable influence on the immunity than the protein-free moiety.