• Proceedings of the Korean Society of Life Science Conference
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• 2003.10a
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• pp.58-59
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• 2003

• 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.

• Microbiology and Biotechnology Letters
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• v.29 no.1
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• pp.25-30
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• 2001

A strain of Actinomycetes producing cathepis B inhibitor was isolated from soil and identified as Streptomyces misakiensis. The product of S. misakiensis inhibited effectively cathepsis B proteinases as well as trypsin and papain. The cathepsin B inhibitor were largely produced with incubation for 4 days. The S. misakiensis was the most growth with incubation for 5 days. The cathepsin B inhibitor was isolated from the extraction of both with ethanol, ethanol and chlorofrom, and following several column chromatography such as sephadex G-15, silica gel 60 and sephadex LH-20 chromatography. The moleculer weight of purfied inhibitor was 138 dalton.

• Microbiology and Biotechnology Letters
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• v.27 no.6
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• pp.458-465
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• 1999

Streptomyces luteogriseus KT-10 isolated from Korean farm soil produced a strong cathepsin B inhibitor. Optimal conditions for the cathepsin B inhibitor production by s. luteogriseus KT-10 were evaluated. The cathepsin B inhibitor was produced with maximal yield in the cultural condition of pH 7.0 and $25^{\circ}C$ for 4 days. Optimal medium for the cathepsin B inhibitor production was determined to be a medium containing 20g, peptone 3g, yeast extract 1g, K2HPO4 0.5g, MgSO4.7H2O 0.5g, NaNO3 0.5g, NaCl 0.5g per l. The cathepsin B inhibitor produced by S. luteogriseus KT-10 could also inhibit the other proteinases such as trypsin, papain, and cathepsin D.

• Applied Biological Chemistry
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• v.32 no.2
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• pp.116-125
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• 1989

Bowman-Birk type protease inhibitors of soybeans were purified with gel filtration on Sephadex G-75. Significant differences were found in the content and in the electrophoretic patterns of the purified protease inhibitors. Ten among fourteen electrophoretic bands appeared as protease inhibitors. The chymotrypsin and trypsin inhibiting activities in soybeans showed three and four fold variation respectively. And the cultivars with higher chymotrypsin inhibiting activities seemed to have higher cysteine contents.

• Research in Plant Disease
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• v.19 no.2
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• pp.114-117
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• 2013

To facilitate their spread, plant viruses have developed several methods for dispersal including insect and seed transmission. While insect transmission requires virus stability against insect digestion, seed-transmitted viruses have to overcome barriers to entry into embryos. Bean pod mottle virus (BPMV) is transmitted through seed at levels typically below 0.1%, but co-infection with Soybean mosaic virus (SMV) enhanced the seed transmission rate of BPMV in one experiment. In contrast, the rate of SMV seed transmission was not affected by BPMV co-infection. In a second preliminary study, the rate of SMV transmission was lower in an isoline of Williams 82 that contained a null mutation for the Kunitz trypsin inhibitor gene than in Williams 82. In this preliminary study, we observed that factors such as protease inhibitor expression and dual infection may affect the frequency of seed transmission of BPMV and SMV.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.29 no.6
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• pp.797-804
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• 1996

Two trypsins were purified from shrimp hepatopancreas through ammonium sulfate fractionation, Q-Sepharose ionic exchange, benzamidine Sepharose-6B affinity, and Sephacryl S-300 gel chromatography. Both enzymes had a single polypeptide chain with a molecular weight (M.W.) of 32 kDa by sodium dodecylsulfate polyacrylamide gel electrophoresis (SOS-PAGE), although trypsin A and B were estimated to be a molecular weight of 27.2 and 22.8 kDa, respectively, using Sephacryl S-300 gel filtration. Both trypsins had similar amino acid compositions and rich in glycine, valine, alanine, aspartic acid, and glutamic acid, but low in methionine and basic amino acids. Both enzymes were completely inactivated by soybean trypsin inhibitor (SBTI), phenylmethylsulfonyl fluoride (PMSF), tosyl-L-lysine chloromethyl ketone (TLCK), benzamidine, leupeptin, however, not affected by tosyl-L-phenylalanine chloromethyl ketone (TPCK) and pepstatin.

• The Korean Journal of Pain
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• v.26 no.4
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• pp.356-360
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• 2013

Background: Nerve injury sometimes leads to chronic neuropathic pain associated with neuroinflammation in the nervous system. In the case of chronic neuropathic pain, the inflammatory and algesic mediators become predominant and result in pain hypersensitivity following nervous system damage. It is well known that urinary trypsin inhibitor (ulinastatin, UTI) has an anti-inflammatory activity. Recently, the neuroprotective action of UTI on the nervous system after ischemic injury has been reported. Thus, we evaluated the neuroprotective effect of ulinastatin in a rat model of neuropathic pain. Methods: Neuropathic pain was induced with L5 spinal nerve ligation (SNL) in male Sprague-Dawley rats weighing 100-120 g. The rats were divided into 3 groups, with n = 8 in each group. The rats in the control group (group 1) were administered normal saline and those in group 2 were administered UTI (50,000 U/kg) intravenously through the tail vein for 3 days from the day of SNL. Rats in group 3 were administered UTI (50,000 U/kg) intravenously from the $5^{th}$ day after SNL. The paw withdrawal threshold was measured using the von Frey test for 3 days starting from the $5^{th}$ day after SNL. Results: The paw withdrawal thresholds were significantly increased in the rats of group 2 compared to the other groups (P < 0.05). Conclusions: Ulinastatin, which was administered for 3 days after SNL, increased the paw withdrawal threshold and it could have a neuroprotective effect in the rat model of neuropathic pain.

• Journal of Aquaculture
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• v.5 no.1
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• pp.1-7
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• 1992

Digestion rates of protein, carbohydrate, and lipid in the two kinds of extruding processed soybean meals, heated (H-SBM) and raw (R-SBM), were tested for evaluate the effectiveness of soybean meal in the rainbow trout diet. The relation between digestion rate of protein and trypsin inhibitor (TI) was also determined. The protein digestion rate of both H-SBM and R-SBM were increased up to $95{\%}$ by extruding process compared to the none treated soybean meal. The digestion rate of carbohydrate in R-SBM was increased by extruding process whereas the one in H-SBM was not. The activity of trypsin inhibitor was almost diminished by the extruding process and digestion rate of dietary protein was improved. However, the reason of this improvement was not clear whether caused by the deactivation of trypsin inhibitor.

• Journal of Crop Science and Biotechnology
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• v.10 no.3
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• pp.159-162
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• 2007

Soybean Kunitz trypsin inhibitor(SKTI) protein is a small, monomeric and non-glycosylated protein containing 181 amino acid residues and is responsible for the inferior nutritional quality of unheated or incompletely heated soybean meal. The objective of this research is to confirm SSR marker(Satt228) tightly linked to the Ti locus using several germplasm accessions with TiTi or titi genotypes for MAS in soybean breeding programs. TiTi genotypes('Jinpumkong2', 'Clark', and 'William') had allele1 and titi genotypes(PI196168, C242, W60, and PI157440) had allele2 in Satt228 marker analysis. 'Jinpumkong2', 'Clark', and 'William'(TiTi genotype) had a Kunitz trypsin inhibitor protein of 21.5 kDa size, and PI196168, C242, W60, and PI157440(titi genotype) did not have the band in protein gel electrophoresis from the mature seed. Cosegregation between the SKTI protein(21.5 kDa size) and allele of Satt228 marker was observed in seven germplasm accessions with different genetic backgrounds. Any recombination between the SKTI protein and allele of the Satt228 marker was not observed. This result indicates that Satt228 marker may effectively utilized to select the plants with the titi genotype.