• Journal of Nutrition and Health
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• v.12 no.4
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• pp.11-19
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• 1979

A numerical analysis of essential amino acid pattern of protein in daily Korean foods was conducted through computer programming based on the food intake data from 'Reports of national nutritional survey (1969, $1973{\sim}1979)'$ and food supply data from 'Food balance sheet $(1970{\sim}1977)'$. It was noted that the amounts of daily intake and supply of animal protein were gradually increased since 1973. In 1977, animal protein intake was 17.5g in total protein intake of 68g per person per day. Intake and supply of total essential amino acids were $20{\sim}28g$ per person per day in the both of urban and rural areas, and greater consumption of leucine, phenylalanine+tyrosine, isoleusine, lysine and valine was observed. Amino acids scores of consumed protein based on FAO provisional amino acid scoring pattern(1973) were around $75{\sim}90$ showing the scores of 77.9 in 1969 and 89.5 in 1977, and also lysine(1969, $1973{\sim}1976$) and threonine(1977) were considered as first limiting amino acid. On the other hand the scores of supply Protein $(1970{\sim}1977)$ rated in $82{\sim}88$, lysine$(1970{\sim}1971)$ or threonine $(1972{\sim}1977)$ was found as first limiting amino acid. Generally a protein quality of Korean daily food was improved since 1973 and a difference between urban and rural areas in terms of the nutritive quality of protein was considerably reduced in 1977.

• Nutrition Research and Practice
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• v.3 no.1
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• pp.64-71
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• 2009

Amino acids are fundamental nutrients for protein synthesis and cell growth (increase in cell size). Recently, many compelling evidences have shown that the level of amino acids is sensed by extra- or intra-cellular amino acids sensor(s) and regulates protein synthesis/degradation. Mammalian target of rapamycin complex 1 (mTORC1) is placed in a central position in cell growth regulation and dysregulation of mTOR signaling pathway has been implicated in many serious human diseases including cancer, diabetes, and tissue hypertrophy. Although amino acids are the most potent activator of mTORC1, how amino acids activate mTOR signaling pathway is still largely unknown. This is partly because of the diversity of amino acids themselves including structure and metabolism. In this review, current proposed amino acid sensing mechanisms to regulate mTORC1 and the evidences pro/against the proposed models are discussed.

• Journal of Microbiology and Biotechnology
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• v.6 no.6
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• pp.369-374
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• 1996

The ${\beta}$-lactamase inhibitory protein (BLIP) produced by Streptomyces exfoliatus SMF19 was purified(33 kDa) and the N-terminal amino acid sequence was determined as NH2-ATSVVAWGGNND. Genomic DNA library of S. exfoliatus SMF19 was constructed in pWE15 and recombinants harbouring the corresponding gene were selected by colony hybridization to the mixture of 36-mer oligonucleotide designed from the N-terminal amino acid sequence. The corresponding gene (bliX) was isolated on a 4-kb ApaI fragment of S. exfoliatus SMF19 chromosomal DNA and then sequenced. The bliX consisting of 1, 119bp encoded a mature protein with a deduced amino acid sequence of 342 residues and also encoded a 40-amino-acid signal sequence. No significant sequence similarity to bliX was found by pairwise comparison using various protein and nucleotide sequences.

• Preventive Nutrition and Food Science
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• v.3 no.2
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• pp.175-179
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• 1998

Some functional properties and nutritive value were determined for the protein concentrated fractionated from chrysanthemum flower in orer to renew interest in the flowers as food. Proximate components of chrysanthemum flower protein concentration (FPC) showed 61.2% protein, 2.0% fat and 35.2% carbhydrate on a dry basis. In amino acid composition of FPC, glutamic acid was the highest in the content, follwoed by aspartic acid, leucine and lysine. The ratio of essential/ total amino acids(E/T) was 0.42, showing a higher level of essential amino acids compared to the FAO reference protein. Digestibility of chrysanthemum FPC by pepsin and trypsin was lwoer than that of casein and was negatively correlative to both water and fat absorptions. Similar characteristics were determined between chrysanthemum FPC and milk casein in their emulsifying activity and emulsion stability. This results indicate that flowers or petals of chrysanthemum might be developed as a good source of protein.

• Plant Resources
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• v.1 no.2
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• pp.92-97
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• 1998

An isolate of barley yellow mosaic virus(BaYMV-HN) obtained from Haenam, Korea was compared with two BaYMV strains. BaYMV-Ⅱ-1 from Japan and BaYMV-G from Germany. The sequence of the 3'-terminal 3817nucleotides[excluding the poly (A) tail] of RNA 1 of BaYMV-HN was determined to start within a long open reading frame coding for a part of the NIa-VPg polymerase(26 amino acids). NIa-Pro polymerase (343 amino acids), NIb polymerase(528 amino acids) and the entire capsid protein(297 amino acids), which is followed by a noncoding region(NCR) of 235 nucelotides. In the partial ORFs, BaYMV-HN shows higher sequence homology with BaYMV-Ⅱ-1(99.5%) than BaYMV-G(92.7%). The 3' non-coding regions of BaYMV-HN(235nt) shows higher nucleotide sequence homology with BaYMV-G(235nt)(99.6%) than BaYMV-Ⅱ-1(231nt)(97.0%). The 3' NIa-Pro protein sequence of BaYMV-HN shows higher amino acid sequence homology with BaYMV-Ⅱ-1(95.0%) than BaYMV-G(93.6%), but, NIb protein sequence of BaYMV-HN shows same all amino acid sequence. The capsid protein sequence of BaYMV-HN(297aa) shows same with BaYMV-Ⅱ-1, and shows higher nucleotide sequence homology with BaYMV-UK (from United Kingdom)(97.3%) than BaYMV-G(96.9%) and G2(96.9%). Difference of capsid protein amino acid were 0-9 between the Japan, United Kingdom and Germany and were 2-6 between all Korean isolates. Many of the amino acid differences are located in the N-terminal regions of the capsid proteins from 1 to 74 amino acid positions.

• Journal of Sericultural and Entomological Science
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• v.21 no.2
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• pp.7-10
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• 1979

Purified preparations of flacherie virus capsid protein were fractionated by SDS-polyacrylamide gel electrophoresis, and amino acid composition was determined by amino acid analyzer. Three polypeptide components, FP I, FP II and FP III were detected, and the molecular weights of these components were 37,500, 30,500 and 26,500 respectively. The FP III was major poly-peptide comprised about 68.4% of the total virus capsid protein. Seventeen amino acids were detected by an amino acid analyzer from hydrolyzate of the virus capsid protein and the pattern of amino acid composition was similar to those of several other insect viruses.

• Asian-Australasian Journal of Animal Sciences
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• v.7 no.4
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• pp.537-546
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• 1994

This experiment was carried out to compare the effects of six different plant protein sources such as soybean meal, extruded full-fat soybean, canola meal, rapeseed meal, cottonseed meal and perilla meal as a sole protein source of diets on growth performance and amino acid bioavailabilities in growing-finishing pigs. A total of 54 pigs with average 25 kg of body weight were used as experimental subjects for a 65-d feeding trial. Digestion trial was carried out with seven ileal-cannulated pigs. The most rapid rate of weight gain was observed in pigs fed soybean meal and full-fat soybean, the moderate one in pigs fed canola meal and cottonseed meal and the least one in pigs fed rapeseed meal and perilla meal (p<0.005). Feed efficiency was better for groups fed soybean meal and full-fat soybean than other protein meals (p<0.05). The apparent ileal digestibilities of essential amino acids of soybean meal and full-fat soybean (82.5% and 81.6%) were significantly (p<0.05) higher than those of other protein sources (61.2 to 69.4%). Regardless of protein sources, the apparent ileal digestibility of arginine was highest, whereas that of histidine was lowest among essential amino acids. Proline had the lowest digestibility among non-essential amino acids. True amino acid digestibilities tended to be higher than apparent amino acid digestibilities. The differences between true and apparent ileal digestibilities were greater in canola meal, rapeseed meal or cottonseed meal than other protein sources. The differences was greatest in praline except for cottonseed meal. The fecal digestibility appeared to be higher than the ileal digestibility. The differences between fecal and ileal digestibilities were greater in canola meal, rapeseed meal, cottonseed meal and perilla meal than in soybean meal and full-fat soybean. In general, praline was the most disappeared amino acid in the hind gut, while the net synthesis of lysine in the large intestine was observed in all protein sources except perilla meal. It is appropriate that swine feeds should be formulated based on true ileal amino acid digestibility of protein sources for pig's normal growth.

• Journal of Ginseng Research
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• v.14 no.1
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• pp.21-26
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• 1990

The chemical composition and stabilities of the purified ginseng invertase were investigated. The purified enzyme was found to be a glycoprotein composed of 80.2% protein and 19.7% total sugar. The protein component of the enzyme was composed of acidic amino acid (9.3%), basic amino acid (48.9%), nonpolar amino acid (21.4%), polar amino acid (20.4%) and 6.1% S-containing amino acid. It showed especially high contents of histidine and serine. The enzyme was inactivated almost completely by the treatment with some proteases (papain, pepsin. trypsin, pancreatin and microbial alkaline pretense) and protein denatllrants (8M urea and 6M guanidine-HC1), bolt not with glyrosidase (${\alpha}$-amylase, ${\beta}$-amylase. glcoamylese and cellullase). btonosaccharides sllch as glilrose, fructose, galactose and mannose did not exert any influence on the enzyme activity. The activity of the enzyme was inhibited by Ag+, Mn2+, Hg2+, Zn2+ and Al3+, whereas Ca2+, Mg2+, Ba2+ and Fe3+ gave rather activating effects on the enzyme activity. The enzyme was relatively stable in the VH range of VH 6 and 8, and at the temperatures below 35$^{\circ}C$.

• Journal of Korean Society of Forest Science
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• v.6 no.1
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• pp.43-48
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• 1967

In the present experiment the amino acid composition in the pollen of Pinus taeda and Pinus rigida and methbolic changes of the composition occurring in germinating pollen were examined by the method of paper chromatography. The results obtained in this study are as follows. 1. The mature pollen of Pinus taeda and Pinus rigida contained 12.00%, 13.19% crude protein respectively and sixteen protein-constituting amino acids and three unknowns were detected on the chromatogram. 2. Main components of the protein-constituting amino acids were leucines, valine, alanine, glutamic acid and aspartic acid. 3. The free amino acids such as leucines, valine, tyrosine, alanine and glutamic acid increased evidently during germination of the pine pollen.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.14 no.2
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• pp.66-71
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• 1981

In order to study the decomposition process of glycogen and protein of oyster during fermentation with salt, and the relationship between their breakdown products, the amounts of free reducing sugars and lactic acid were determined, and amino acid compositions were analysed. In addition, the amount of the available lysine which may help us to estimate the reaction of the free reducing sugars with the free amino acids was also determined. Glycogen and protein were gradually decomposed to free reducing sugars and lactic acid, and free amino acids, respectively, and the available lysine was slightly decreased during the fermentation process. Glutamic acid, aspartic acid, lysine and proline were relatively rich in the amino acid com-position of raw oyster protein while amino acids such as tryptophan, methionine, histidine and tyrosine were poor. It was noted that the decreased amino acids in the protein from the fermented oyster were valine, histine, isoleucine and lysine. As a respect to the free amino acids, proline, taurine, glycine, glutamic acid and alanine were abundant in the raw oyster and reached up to $69\%$ of the total fret amino acids. In the fermented oyster, proline, glutamic acid, glycine, alanine, aspartic acid and lysine were prevalently contained and marke about $65\%$ of the total free amino acids. The contents of free amino acids such as lysine, arginine, aspartic acid, glutamic acid, cysteine, isoleucine and tyrosine increased during fermentation while those of taurine, proline and leucine decreased.