• Proceedings of the Korean Society of Applied Pharmacology
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• 1995.10a
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• pp.39-40
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• 1995

Thymopoietin(TP) was originally isolated from bovine thymic extracts on the basis of its ability to affect neuromuscular transmission when injected into mice (Goldstein, 1974). A 49 amino acid polypeptide was isolated and sequenced (Schlesinger and Goldstein, 1975). It is now evident that this molecule was created by proteolytic cleavage of larger thymopoietin proteins during isolation, and represents the N-terminal sequence of these proteins. Nevertheless, this proteolytic fragment was active in both neurophysiological and immunological experiments, and enabled the identification of an active pentapeptide. (amino acids 32 to 36, Arg-Lys-Asp-Val-Tyr, thymopentin), which. has been studied as an immunomodulatory drug.

• Korean Journal of Pharmacognosy
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• v.30 no.3
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• pp.314-319
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• 1999

The composition of biochemical components such as lipids, proteins and their amino acid components and inorganic elements in the ashes in unossified antlers from Cervus nippon Temminck var. mantchuricus grown in Korea were analyzed to obtain fundamental data for quality control. As a result, it was found that total lipids were 20.75% which was approximately similar contents with those of proteins (21.8%). Sixteen amino acids were identified from the hydrolysate of the protein fraction. Three gangliosides with very similar TLC patterns of those such as $GM_3$, $GM_1$ and $GM_{1a}$ were identified from the water soluble layer of Folch's partitions. Ash contents were revelaed to be much higher in the sponge layer (40.0%) than in the velvet layer (3.7%).

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

• Food Science and Preservation
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• v.8 no.2
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• pp.187-192
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• 2001

Amino acid composition of proteins in Italian millet, Common millet and sorghum were invstigated by HCI hydrolysis method. The optimum condition was obtained by hydrolysis at 110$\^{C}$ for 24hr. As major amino acids from protein hydrolyzate, the content of tyosine, arginine and phebylalanine were 7.06%, 6.79% and 6.44%, respectively. The content of glutamic acid in Common millet, Italian millet and Sorghum were 5.73%, 5.64% and 5.46%, respectively. Glycine content was about 2.93% in three samples. Contents of crude protein and pure protein in Italian millet, Common millet and sorghum were determined by micro-kjeldahl method. Crude protein contents were slightly higher than that of pure protein. Protein content of sorghum was higher than those of Italian millet and Common millet. For SDS-PAGE analysis, Italian millet showed more soluble proteins including 50kDa, 30kDa and smaller proteins than other cereals. In particular, Common millet and Sorghum only solubilized proteins less than 15kDa.

• Molecules and Cells
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• v.42 no.5
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• pp.386-396
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• 2019

Labeling of a protein with a specific dye or tag at defined positions is a critical step in tracing the subtle behavior of the protein and assessing its cellular function. Over the last decade, many strategies have been developed to achieve selective labeling of proteins in living cells. In particular, the site-specific unnatural amino acid (UAA) incorporation technique has gained increasing attention since it enables attachment of various organic probes to a specific position of a protein in a more precise way. In this review, we describe how the UAA incorporation technique has expanded our ability to achieve site-specific labeling and visualization of target proteins for functional analyses in live cells.

• Journal of the Korean Chemical Society
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• v.8 no.4
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• pp.164-168
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• 1964

We isolated histone-type basic proteins from lemna paucicostata for the first time. Basic proteins were extracted directly with dilute mineral acids from homogenized lemna paucicostata. Amino acid compositions of basic protein portions adsorbed on Amberlite CG-50(at pH 6. 0) were resembled to those of calf thymus histones. Especially, lysine content was the greatest of the other amino acids. By chromatographic studies, adsorbed portions of basic protein components on carboxymethyl cellulose column(at pH 4. 2) were shown to be homogeneous to calf thymus histones, however, the area under the individual curve was different, and furthermore, the containing of a non-adsorbed portion in the large extent was markedly different from calf thymus histones. And amino acid compositions of adsorbed portions represented the histone-type basic propertes, but non-adsorbed portions were considered as a different protein compared with the typical histone. When calf thymus histone and protein components separated from lemna paucicostata were heated($60^{\circ}C$) with a solution of $HgSO_4-H_2SO_4$, precipitates were not obtained.

• YAKHAK HOEJI
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• v.31 no.4
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• pp.224-229
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• 1987

The earthworm(Annelid) is a herbicine which has traditionally been used in the treatment of infectious fever, jaundice, infection of middle ear, laryngitis, pharyngitis, nephritis, headache, toothache and certain urinary tract infections from the olden times. Before the isolation and purification of biologically active components we analyzed the basic constituents(proteins, amino acids, mineral, etc.) with lyophilized powder of Lamnodrilus gotai Hatai. The results were as follows: Minerals detected and quantitatively analyzed were $Ca^#$, $Mg^#$, Fe, Zn, Mn, Cu, Co, Cr, Ni, Ge and Se. Amino acids detected were alanine, phenylalanine, leucine, glutamic acid, tyrosine, threonine, arginine, aspartic acid, methionine, lysine, serine, histidine, isoleucine, glycine, proline and etc. The constituents of proteins, fat, fiber, ash and phosphorous were measured. These constituents were compared and discussed with those of other investigations.

• Food Science of Animal Resources
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• v.34 no.1
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• pp.1-6
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• 2014

Pidan and salted duck eggs are of nutritional rich alternative duck egg products which are predominantly consumed in China, Thailand, South Korea and other Chinese migrated countries. Both eggs are rich in proteins, lipids, unsaturated fatty acids and minerals. A Pidan whole egg contains 13.1% of protein, 10.7% of fat, 2.25% of carbohydrate and 2.3% of ash, whereas the salted duck egg contains 14% of protein, 16.6% of fat, 4.1% of carbohydrate and 7.5% of ash. The fresh duck egg contains a range of 9.30-11.80% of protein, 11.40-13.52% of fat, 1.50-1.74% of sugar and 1.10-1.17% of ash. Proteins, lipids, and ash contents are found to be greatly enhanced during the pickling and salting process of pidan and salted duck eggs. However, the alkaline induced aggregation of pidan leads to degradation and subsequent generation of free peptides and amino acids. Very few amino acids are found to be lost during the pickling and storage. However, no such losses of amino acids are reported in salted duck eggs during the salting process of 14 d. Phospholipids and cholesterol contents are lower in pidan oil and salted duck egg yolk oil. Thus, the pidan and salted duck eggs are nutritionally rich alternatives of duck egg products which will benefit the human health during consumption.

• Korean Journal of Microbiology
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• v.11 no.2
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• pp.79-88
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• 1973

In order to investigate the effect of gamma radiation on Salmonella typhi, Ty2, the components of amino acids, proteins, carbohydrates and lipids in irradiated cells were compared with those in unirradiated control cells respectively. The results obtained were as follows ; 1) The inactivation curves of Salmonella typhi with $Co^{60}$ .gamma.-ray irradiation were exponential over a wide range to the irradiated doses. 2) Dose for the inactivation factor of $10^8$ was 94.0 Krad in physiological saline or in phosphate buffered saline, 104.2 Krad in nutrient broth, 220.4Krad in frozen state, 552.0 Krad in dried state, 88.3 Krad in the abundance of oxygen and 188.0 Krad in the deficience of oxygen, respectively. 3) Five consecutive irradiation of Salmonella typhi suspension at the dose of 90 Krad gave no additional increase in resistance. 4) Even at the smallest dose of 500 Krad, compositions of amino acids, proteins, carbohydrates, and lipids were more or less decreased and the distinct banding patterns were also lost possibly due to degradation of the protein molecules.

• Journal of Microbiology and Biotechnology
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• v.7 no.2
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• pp.132-137
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• 1997

A novel protein (HEAAE, High Essential Amino Acid Encoding Protein), rich in essential amino acids ($75{\%}$ of total), was designed and constructed in our laboratory. The designed peptides were analyzed by SYBLE and stable secondary and tertiary structures were predicted. The monomeric form (HEAAE-1) of the protein consists of 20 amino acid residues with four additional amino acids comprising a potential ${\beta}$-turn (HEAAE-4). Size exclusion analysis demonstrated that the monomer is self-aggregates in aqueous solution to form higher ordered multimeric structures, which are very reminiscent of natural plant storage proteins. The DNA encoding this amino acid sequence was synthesized, and from this monomeric gene fragment (heaae-1), the stable tetrameric form of the gene (heaae-4) was generated by subcloning into the E. coli expression vector pKK223-3. A clear 6 kDa polypeptide band corresponding to the molecular weight of the dimeric form (HEAAE-2) was detected. The smeared band which appeared around the molecular weight corresponding to HEAAE-4 of 11 kDa suggested that the tetramer form of this protein might be processed into smaller size products.