• Proceedings of the PSK Conference
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• 2005.11a
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• pp.101-101
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• 2005

• Bulletin of the Korean Chemical Society
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• v.20 no.2
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• pp.244-246
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• 1999

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.1
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• pp.35-39
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• 1991

Properties of a protease purified from Neungee[Sarcodon aspratus(Berk, ) S. Ito] have been investigated. The enzyme displays a glycosylated serine protease. The enzyme is able to hydrolyze alanine glycine methionine glutamine and cysteine of N-CBZ and N-t-BOC-L-amino acid derivatibes relatively strongly but splits valine proline and isoleucine derivatives with low affinity which means the enzyme has the broad substrate spectrum toward the amino acids. Interestingly the enzyme was inhibited by bromelain inhibitor. That is the active site environ-ment of the enzyme is believed to be similar to that of bromelain However peptide mapping studies show that the two enzymes have distinct different cleavage sites.

• BMB Reports
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• v.29 no.3
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• pp.248-252
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• 1996

The epidermal organ of the leech contains a complex glycoprotein molecule of mucus. The mucus excreted from annelids plays Significant role in protection against desiccation and parasites. Mucus from the Korean native leech, H. nipponia, was investigated for biochemical characteristics for possible development of biomaterials of cosmetic and pharmaceutical agents. The leech skin mucus was heavily glycosylated mucin-like protein with a high molecular weight comprised 80% carbohydrate and 20% protein. Threonine, serine, and glycine were the major components of the isolated protein and these accounted for 50% of total amino acids. The carbohydrate portion contained glucosamine, galactosamine. galactose, glucose. mannose and sialic acid in oligosaccharide form linked with threonine and serine residues of the glycoprotein.

• Korean Journal of Microbiology
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• v.28 no.1
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• pp.65-70
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• 1990

The objective of the current study is to elucidate the biological roles of proteinase inhibitor in microorganisms. As the first step, a strain of Streptomyces fradiae was selected as a producer of extracellular proteinase inhibitor. The proteinase inhibitor was purified from culture broth through ultrafiltration, gel-filtration and ion-exchange chromatography. Molecular weight of the proteinase inhibitor was estimated to be 16, 800 by SDS polyacrylamide gel electrophoresis. It was found that the proteinase inhibitor inhibited only alkaline serine proteinases such as subtilisin, $\alpha$-chymotrypsin and Promase E but not trypsin and other proteinases. The mode of inhibition against Pronase E with succinyl-phenylalanine-p-nitroanilide as a substrate was competitive.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1996.04a
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• pp.165-165
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• 1996

균의 감염에 의해 유도되는 패혈성 shock는 균이 분비하는 elastase가 관여하며, 외부에서 serine pretense inhibitor의 biopolymer의 투여로 균에 의해 유도된 패혈성 shock를 억제시킬 수 있다고 보고되고 있다. 이에 본 연구진은 패혈성 치료제의 개발의 목적으로, 국내에서 민간 약으로 많이 이용되고 있는 백편두로부터 새로운 elastase inhibitor를 분리, 정제하여 부분 아미노산 서열 및 특성을 조사하였기에 발표하고자 한다. 백편두 추출액을 여러 차례에 걸쳐 column chromatography을 수행하면서 얻어지는 각 fraction에 대하여 elastase MCA-기질 및 trypsin MCA-기질을 이용하여 활성 측정 후 elastase 기질 및 trypsin 기질에 대하여 활성을 억제하는 fraction들을 모아 $C_{18}$ open column chromatography 및 $C_{18}$ HPLC 과정을 수행하여 2종류의 trypsin 활성 억제 물질과 1종류의 elastase inhibitor를 분리, 정제하여 각각을 Ti1, Ti2 및 Ti3로 명명하였다. 전기영 동 상에서 단일 hand를 확인한 후 각각의 inhibitor들의 부분 아미노산 서열을 결정하였다.

• Microbiology and Biotechnology Letters
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• v.23 no.1
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• pp.81-86
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• 1995

A Streptomyces strain YS-943, which produced amino acid antimetabolite, was isolated from soil. During the course of screening for new amino acid antimetabolites from the culture broth of Actinomycetes, we found that the strain produced a substance active against Gram-positive bacteria and its activity was reversed by L-methionine and L-histidine on the synthetic minimal agar medium in the culture broth.The morphological and cultural characteristics serve to identify the producing organism strain YS-943 as the genus Streptomyces. Fermentation was carried out in the synthetic medium at 28$\CIRC$C for 48 hours. The fermentation yield reached about 12 mg per liter of the broth. The YS-943 substance was obtained as white powder, mp 194$\CIRC$C and has the molecular formular of C$_{4}$H$_{8}$N$_{2}$O$_{4}$. Its structure was determined to be o-carbamyl-D-serine by spectroscopic data. It is active against some Gram-positive bacteria and reversed by L-methionine and L-histidine.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.12 no.3
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• pp.181-189
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• 1979

1. 전복, 소라, 북방조개, 가리비의 중요한 인지질은 choline phosphatides, ethanolamine phlosphatides, serine phosphatides, cardiolipin, sphingomyelin 및 lyso choline phosphatides 였다. 2. 이들 plasmalogen은 거의 대부분이 ethanolamine phosphatides에 존재하고, choline phosphatides에는 소량존재하였으며, serine phosphatide에는 전연발견되지 않았다. 3. 전복의 ethanolamine plasmalogen 함량은 1월에 채취한 것에는 $3.5\%$, 7월에 채취한 것에는 $17.2\%$였다. 또, 소라, 북방조개에는 각각 그 함량이 $20.7\%,\;15.1\%$였다. 가리비에는 ethanolamine phosphatides에 plasmalogen이 $18.8\%$ 존재하였다. 4. 전복 및 소라의 중요한 plasmalogen의 aldehyde 조성은 stearyl aldehyde $(C_{18:D})$, palmityl aldehyde $(C_{16:0})$, Palmitoleyl aldehyde $(C_{16:1})$ 및 oleyl aldehyde $(C_{18:1})$ 인데 대하여, 2매패인 북방조개, 가리비에는 eicosamonoenal $(C_{20:1})$이 $14-22\%$ 정도함유 되어 있어 권패와 대조적이였다.

• Biomedical Science Letters
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• v.12 no.3
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• pp.225-231
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• 2006

Fibrinolytic enzyme was purified from the fruiting bodies of Lepista nuda, using DEAE-Cellulose chromatography, Phenyl Sepharose chromatography, and Mono-S column chromatography. The substance has a molecular weight of 30006.62 Da as measured by MALD-TOF mass spectrometry. The N-terminal amino acid sequence of the enzyme was Tyr-Pro-Ser-Pro-Ser-His-Gln-Thr-Ala-Val-Asn-Ala-Ile-Ile-X. The activity of the enzyme was inhibited by PMSF, indicating that the enzyme is a serine protease. No inhibition was found with E-64, pepstatin, and EDTA. It has broad substrate specificity for synthetic peptides. The enzyme was stable up to $30^{\circ}C$. The enzyme hydrolyzes both Aa and y chains of human fibrinogen but did not show any reactivity for $B{\beta}$ chain of human fibrinogen.

• The Korean Journal of Zoology
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• v.3 no.2
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• pp.5-8
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• 1960

Paper partition chromatography has been applied to estimate the amino acids in the liver of Bombina orientalis Boulenger. The results obtained are as follows : 1) The presence of cystine, serine, glycine, threonine, alanine, $\beta$-alanine, tyrosine, histidine, asparagine, tryptophane, methionine, valine, phenylalanine, leucine and an unknown substance has been demonstrated in the alcoholic extracts of the material. 2) The presence of glutamine, cystine, serine , glycine, arginine, threonine, histidine, alanine, methionine, proline, valine ,phenylalanine, leucine, and two unknown substances has been demonstrated in the acid-hydrolyzed liver. 3) Tyrosine, asparagine, and trypotphane have been demonstrated only in the alcoholic extract. 4) Proline, glutamine and arginine have been demonstrated only in the acid-jydrolyzed liver.