• BMB Reports
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• v.31 no.2
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• pp.196-200
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• 1998

Zeins, maize storage proteins, are retained in the endoplasmic reticulum (ER) during the subcellular targeting process without the ER retention signal. Circumstantial data indicate that the 27K zein is an ER transmembrane protein. The potential transmembrane domain may permit the 27K zein to remain in the ER. This study investigated the potential transmembrane feature by employing alkaline extraction, proteinase K digestion, and surface biotinylation on isolated intact protein bodies. These assays consistently support the possibility of the 27K zein as a transmembrane protein. The 27K zein polypeptide was shown to be associated with alkali-stripped membranes. The polypeptide was digested by proteinase K to a smaller fragment. According to surface biotinylation, the 27K zeins was labeled to the exclusion of other classes of zeins. This study, therefore, concludes that the 27K zein has an ER transmembrane domain, which may serve as an anchor for zeins' ER retention.

• Microbiology and Biotechnology Letters
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• v.20 no.2
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• pp.207-212
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• 1992

An anti-inflammatory agent, serratiopeptidase, was produced from the culture of the Serratia marcescens. The effects of carbon sources, nitrogen sources and inducers on the production were investigated. Citrate was found to be inhibitory in the production of serratiopeptidase. The enzyme was synthesized in the synthetic medium without inducers, albeit low level of synthesis. But the synthesis was increased by the addition of proteinaceous substrate and leucine. Induction of extracellular proteinase by its end-product was discovered, which is not common in the proteinase synthesis in the bacteria. By the glucose fed-batch culture, we found the possible catabolite repression on the production of serratiopeptidase.

• Journal of Physiology & Pathology in Korean Medicine
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• v.18 no.1
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• pp.110-113
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• 2004

The Baenong-san has long been used for treatment of inflammatory in Korea. In this study, the anti-inflammatory effects of Baenong-san water extract (BWX) were investigated in proteinase-activated receptor-2 (PAR2)-mediated rat paw edema. Paw edema was induced by injection of trypsin or trans-cinnamoyl-LIGRLO-NH₂ (to-NH₂) into hindpaw of rats. BWX (10, 50, 100 and 200mg/kg) was orally administered 1 h before induction of inflammation. At doses of 50, 100 and 200 mg/kg, BWX showed significant inhibition of both change in paw volume and vascular permeability. BWX(100mg/kg) significantly also inhibited PAR2 agonist-induced myeloperoxidase (MPO) activity in paw tissue. This study demonstrated that BWX has an anti-inflammatory action for PAR2-mediated paw edema.

• Proceedings of the Korean Biophysical Society Conference
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• 1999.06a
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• pp.42-42
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• 1999

Metastability in the native form of proteins has been recognized as a mechanism of biological regulation. The strained native structure of serpins (serine proteinase inhibitors) is a typical example. The native strain of serpins is considered to be crucial to their physiological functions, such as plasma proteinase inhibition, hormone delivery, Alzheimer filament assembly, and extracellular matrix remodeling.(omitted)

• YAKHAK HOEJI
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• v.4 no.1
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• pp.39-42
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• 1959

The enzymatic activity of proteinase which was isolated from a shell fish, Veneridae Soxidomus purpuratus Sowerby(Korean name "Gai-jo-gai") was studied, and the obtained results were as follows; (1) The optimum pH of the enzyme was around 7.5 (2) The prohibiting activity of metalic ions for the enzymatic activity was the order of 1/1000M-$Ag^{+}$>1/1000M-$Zn^{++}$>1/1000M-$Cd^{++}$>1/1000M-$Pb^{++}$. (3) Of 3 specimens of the enzyme from heptapancreas, gastro-intestine and crystalline style the highest activity was shown by one from crystalline style.

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2001.11a
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• pp.144-144
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• 2001

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2002.05a
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• pp.175-176
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• 2002

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 1995.06a
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• pp.280-281
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• 1995

• Proceedings of the Zoological Society Korea Conference
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• 1994.10a
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• pp.261.2-261
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• 1994

No Abstract, See Full Text

• Proceedings of the KTCVS Conference
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• 1993.06a
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• pp.46-46
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• 1993