• Korean Journal of Fisheries and Aquatic Sciences
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• v.34 no.4
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• pp.394-402
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• 2001

In order to investigate the composition of dried layer, Porphyra yezoensis cultured at the south coast of Korea, the dried laver was analyzed separately for extractive nitrogen, free and combined amino acids, ATP and related compounds and quaternary ammonium basis using specimens collected monthly from January to April 1998. The extractive nitrogen contents of dried layer extracts were $976\~1,196\;mg/100\;g$ (on dry basis). Twenty-eight to thirty-one kinds of free amino acids were found in the dried laver extracts and their total amounts were 5,648-6,845 mg/100 g (on dry basis). The extracts were rich in free amino acids such as alanine, glutamic acid, taurine, phosphoserine and aspartic acid. Eighteen to twenty-two kinds of combined amino acids from oligopeptides were found in the extracts and their total amounts were $1,194\~1,406\;mg/100\;g$ (on dry basis). The amounts of ATP and related compounds were $111.6\~195.5\;mg/100\;g\;(3.30\~6.00{\mu}mol/g$ on dry basis). Homarine was detected in all samples but glycinebetaine, $\beta$-alaninebetaine and $\gamma$-butyrobetaine disappeared during processing, TMAO was detected in all samples but low TMA was found in some. During processing of dried layer, P. yezoensis, free amino acids, ATP and its related compounds were increased but the other constituents such as combined amino acids, TMAO and TMA and betaines were decreased in all specimens.

• Parasites, Hosts and Diseases
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• v.34 no.2
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• pp.135-142
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• 1996

Antigenic domain of jai or surface protein (p30) of Toxoplosmc Sondii was analyzed after polymerase chain reaction (PCR) of its gene fragments. Hydrophilic or hydrophobic moiety of amino acid sequences were expressed as glutathione S-transferase (G57) fusion proteins. Fragments of p30 gene were as follows: 737, total p30 open reading frame (ORF) ; S28, total ORF excluding N-terminal signal sequence and C-terminal hydrophobic sequence; Al9, N-terminal 2/3 parts of A28; A19, N-terminal 2/3 of S28; P9, C-terminal 2/3 part of S28; Z9. middle 1/3 of S28; and 29, C-terminal 1/3 of S28. respectively. Primer of each fragment was synthesized to include clamp sequence of EcoR I restriction site. PCR amplified DNA was inserted info GST (26 kDa) expression vector, PGEX-47-1 to transform into Escheri,hia coei (.JM105 strain). G57 fusion proteins were expressed with IPTG induction as 63. 54, 45, 45, 35, 36. and 35 kDa proteins measured by SDS-PAGE. Each fusion protein was confirmed with G57 detection kit. Western blot analysis with the serum of a toxoplasmosis patient revealed antigenicity in proteins expressed by T37. S28, and Al9 but not those by Pl8. X9, Y10, and Z9. Antigenicity of p30 seems to be located either in N-terminal 115 part in the presence of middle 1/3 part or in the oligopeptides between margins of the first and second 1/3 parts.

• Analytical Science and Technology
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• v.12 no.4
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• pp.306-311
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• 1999

Changes of silk protein compositions of average molecular weight (Mw) and free amino acid composition to different solubility conditions were studied by SDS-polyacrylamide electropholesis, gel permeation chromatography (GPC), and free amino acid analysis method. We can not detected average molecular weight distribution of different hydrochloric acid (HCl) conditions as SDS-polyacrylamide method, but as using GPC method, molecular weight distribution of 2N-HCl, 1N-HCl and 0.5N-HCl (3 hrs at $110^{\circ}C$ treated) are confirmed Mw 800, 1,500 and 3,700, respectively. The average molecular weight of calcium chroride and calcium chloride-enzyme treated samples are shown Mw 46,800 and 12,500, respectively. The degree of hydrolysis and the composition of the free amino acid in the fibroin hydrolysates effected significantly composition of free amino acids of the fibroin powder. The increase of the degree of hydrolysis and ratio of free amino acids and oligopeptides were found to be directly related to the concentration of hydrochloric acid and treatment of enzyme, resulting in the increase of water solubility.

• Applied Biological Chemistry
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• v.6
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• pp.107-117
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• 1965

(1) In order to study the specificity of Aspergillus soya protease to soybean protein, as well as the types of peptides formed during soybean-koji prerapation the amino acid sequence for the di & tripeptide and N-terminal amino acid residue and C-terminal amino acid residue were identified. As the results of the study, the following were obtained. Gly, Glu. Ala. Ser. Glu. Ser. Ala. Val (Cys, Glu, Ser, Ala, Arg, Try, Leu or Ileu) Asp. Phe (His, Arg, Cys, Asp, Ser, Ala, Leu or Ileu) Glu. Ala (Cys, Gly, Met) Glu. Ala (Asp, Glu,) Gly. Met (Asp, Glu, Ala, Tyr, Leu or Ileu, Lys,) Gly. Leu or Ileu (His, Asp, Glu, Gly, Ser, Lys, Thr, Phe,) Cys. Gly (Asp, Tyr,) Glu. Pro (Asp, Glu, Ser, Gly, Thr, Ala, Val, Leu or Ileu) Try. Ser (Gly, Glu, Arg, Ala, Met, Leu or Ileu,) Asp. Met (Asp, Glu, Ala, Try, Pro, Leu or Ileu,) His Thr (Ser, Gly, Tyr, Pro, Leu or Ileu,) Glu. Gly (Asp, Ala, Ser, Glu,) Leu or Ileu (2) It has revealed that Aspergillus soya protease has considerably wider range of specificity than that of chymotrypsin, pepsin and trypsin but not mold protease and Aspergillus saitoi protease. It can be said that Asp. soya protease split the bond adjacent to glutamic acid, aspartic acid, glycine, serine, alanine, cystine, tryptophan, histidine preferably acidic amino acid as C-terminal amino acid residue.

• Korean Journal of Food Science and Technology
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• v.31 no.1
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• pp.13-19
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• 1999

In order to investigate the composition and the actual status of extractive nitrogenous compounds in the fresh 'Gae-bul' (echiuroid), a kind of echiurida (Urechis unicinctus), the extract was analyzed separately into extractive nitrogen, free amino acids (FAAs), oligopeptides, nucleotides and related compounds, quaternary ammonium bases, and guanidino compounds, using specimens collected at fish market in April 1988. The extractive nitrogen of echiuroid was $601{\sim}610mg/100g$. Thirty-two kinds of FAAs were found, and the total of them in it was $2,437{\sim}2,609\;mg$. Glycine, alanine, taurine, and serine were the major FAAs in the echiuroid extracts. The large amount of glycine $(1,075{\sim}1,171mg)$ was noted in the extract. The sum of ATP and its related compounds was $3.04{\sim}3.12\;{\mu}mol/g$, and predominant compound was the AMP. Besides, CTP, GTP, UTP and their related compounds were also detected, and the total amount of them was $1.92{\sim}3.74\;{\mu}mol/g$. The lower homarine, trigonelline, TMAO, TMA, and creatine were detected in the extracts. The extractive nitrogenous constituents of medium size and large size echiuroid were almost the same level each other. The total nitrogens of the compounds analyzed for each samples accounted for more than 90% of the extractive nitrogen in this study.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.32 no.2
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• pp.175-179
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• 1999

Processing conditions for dried condiments with oyster, pen shell and cockle shell were investigated. The enzymatic hydrolysis for 3 hours was more profitable than hydrothermal extraction to develop flavoring matters from oyster, pen shell and cockle shell. As a result of omission tests, nucleotides were predominated in the taste compounds of shellfish hydrolysates rather than free amino acids, and the contribution of nucleotides and free amino acids to the taste of shellfish hydrolysates was remarkable. The major flavoring components of shellfish hydrolysates were free amino acids and oligopeptides below 500 dalton. When shellfish hydrolysates were separated with membrane (molecular weight cutoff 500 dalton) for recovering flayer, recovering yields of amino type nitrogen were $92.1\~92.8\%$. Moisture contents of dried shellfish condiments prepared with pretense hydrolyzed oyster, pen shell and cockle shell were $3.5\%,\;3.8\%$ and $3.7\%$, respectively. Contents of total nitrogen were $69.4\%,\;78.8\%$ and $74.2\%$, and those of amino nitrogen were $45.5\%,\;48.9\%$ and $45.4\%$, respectively. Drying yield, solubility and absorption rates at Aw 0.88 were $11.7\%,\;78.4\%$ and $6.8\%$ in oyster, $8.2\%,\;73.6\%$ and $6.1\%$ in pen shell, $9.8\%,\;76.9\%$ and $6.6\%$ in cockle shell, respectively.

• Korean Journal of Food Science and Technology
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• v.27 no.4
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• pp.471-477
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• 1995

Extractive nitrogen, free amino acids, oligopeptides, nucleotides and related compounds, quaternary ammonium bases, and guanidino compounds were analyzed to evaluate quality of anchovy sauce. The commercial products contained low proximate composition, extractive nitrogen and other extractive components, than the experimentally prepared anchovy sauce. Both samples, commercial products and experimentally prepared anchovy sauce, were rich in free amino acids, such as glutamic acid, leucine, alanine, lysine, and aspartic acid. The extractive nitrogenous components which consist of total nucleotides and related compounds, total free amino acids, methionine, isoleucine, valine, taurine, tyrosine, histidine, leucine, aspartic acid, cystine, and lysine, showed significant correlation(p<0.01) with extractive nitrogen. Possibly, seven kinds of free amino acids such as methionine, isoleucine, valine, taurine, tyrosine, histidine, and leucine, might be recommend as quality indices of standardization for anchovy sauce.

• Tuberculosis and Respiratory Diseases
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• v.39 no.4
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• pp.310-317
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• 1992

Background: Angiotensin converting enzyme is a glycoprotein peptidyldipeptide hydrolase which cleaves the c-terminal dipeptides of several oligopeptides. It is a menbrane-bound protein mainly synthesized by the endothelial cells. Since the lung has the largest capillary bed of any organ in the body, it is here that ACE acts on circulating substrates like angiotensin I and bradykinin. It is well known that ACE correlates with disease activity in sarcoidosis and also there are reports that changes in serum ACE activity are found in many acute and chronic lung diseases. So we planned this study to see if serum ACE activity can act as a prognostic factor in lung cancer. Methods: Forty-one newly diagnosed lung cancer patients were included in the study group. There were 19 patients with squamous cell lung cancer, 13 with adenocarcinoma, and 9 with small cell carcinoma. Patients were excluded from the study if they had high blood pressure, heart disease, liver disease, renal disease, or other lung disease. Serum ACE activity was analyzed according to cell type, staging, mode of treatment, and clinical response to treatment. Results: 1) There was no difference in serum ACE activity between lung cancer patients and the control group. Also no difference in serum ACE activity was found according to cancer cell type or staging. 2) In patients who underwent curative resection of lung cancer, serum ACE activity was decreased significantly after the operation. 3) In patients who were diagnosed as non-small cell lung cancer and were treated with 4 cycles of anti-cancer chemotherapy without clinical improvement, changes in serum ACE activity were not seen after the treatment. 4) In patients diagnosed as small cell lung cancer treated with 4 cycles of anti-cancer chemotherapy with clinical improvement, changes in serum ACE activity were also not observed. Conclusion: Serum ACE activity was decreased after lung resection but had no relation to cell type, staging, or clinical response to treatment in lung cancer patients. Therefore, serum ACE activity is not suitable in predicting clinical outcome of lung cancer patients.