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활성형 Vitamin D₃ 전환능을 소유한 방선균에서 P-450 Hydroxylase유전자의 클로닝 전략
서주원,현창구,김정미,김승영,홍순광 명지대학교 자연과학연구소 1998 자연과학논문집 Vol.17 No.-
비타민 D₃는 포유동물이나 새의 간에서 25-hydroxyvitamin D₃[25(OH)D₃]로 전환되는데, 이 hydroxylation은 P-450 hydroxylase에 의해 촉매된다고 알려져있다. 본 연구에서는 활성형 비타민 D₃전환능을 소유한 방선균에서P-450 hydroxylase효소를 신속하게 분리가능한 PCR방법을 보고하고자 한다. Primer는 방선균에서 보고된 P-450 hydroxylase들 사이의 아미노산 서열의비교를 통해 산소결합부위와 heme-ligand pocket 주의에서 제작되었고,5종의 방선균에서 효과적으로 PCR증폭산물을 획득할 수 있었다. 증폭산물을 획득할 수 있었다.증폭 산물들의 아미노산서열을 분석한 결과 기존에 밝혀진 많은P-450 hydroxylase유전자들과 상동성을 보이고 있었으며, 특히 Streptomyces griseolus에서 분리되어 sulfonylurea 등의 제초제의 분해능력을 가진 SuaC, SubC 효소 등과 높은 아미노산 상동성을 지니고 있었다. 이러한 PCR전략은 방선균에서 유용한 물질의 대사에 관여하는 P-450 hydroxylase효소의 클로닝에 도움을 줄 것이라 사료된다 In mammals and birds, vitamin D₃is converted to 25-hydroxyvitamin D₃[25(OH)D₃] and then to 1α25-dihydroxyvitamin D₃[25(OH)₂D₃]in the liver and kideny, respectively these hydroxylating reactions are known to be catalyzed by P-450 hydroxylases. In this paper we report a PCR method which can be used for the repid amplification of DNA fragments for _450 hydroxylase from actinomycetes which can convert to active from of vitamin D₃. Primers were designed based on several regions sharing strong similarities in amino acid sequence of P-450 hydroxylases from a variety of actinomycetes, primarily in the regions of an oxygen binding site and a heme ligand pocket. These primers were used to amplify DNA fragments from five different actinomycetes. The deduced amino acid sequences of the isolated fragments revealed significant similarities to known P-450 hydroxylase including the product of the suaC or subC genes from Streptomyces griseolus that is capable of metabolizing a number of sulfonylurea herbicides and to the product of the P450sca2 from S. carbophilus that produces a specific HMG-CoA reductase inhibitor. This method will be helpful for the researchers in cloning the genes for P-450 hydroxylase involved in the biosynthesis of useful compounds.
Streptomyces coelicolor에서의 이차대사산물 생산조절
홍순광,유재은 명지대학교 자연과학연구소 1996 자연과학논문집 Vol.13 No.-
방선균의 이차대사산물 생산 및 세포분화의 연구대상으로 가장 많이 연구되고 있는 Streptomyces coelicolor에서, actinorhodin 및 undecylprodigiosin과 같은 이차대사산물 생산을 전사단계에서 positive하게 조절하는 global 한 조절유전자 AfsR을 클로닝하여, 이가 코드하는 단백질 AfsR의 기능을 조사하였다 AfsR 단백질은 세포내에 존재하는 인산화효소(kinase)에 의하여 인산화된으로서 활성화되어 이차대사 생산의 조절을 담당하고 있는 것으로 판단된다. 이와같은 AfsR 단백질의 인산화 잔기의 정체를 규명하기 위하여, 인산화된 AfsR 단백질의 여러조건에서의 안정성 및 단백질인산화효소 저해제에 의한 효과를 조사하여 보았다. 그 결과 AfsR 단백질의 인산화 잔기는 산, 알칼리, hydoxylamine, pyridine 등의 처리에 비교적 높은 안정성을 보였고, 많은 종류의 인산화효소 저해제의 처리 결과, 진핵생물의 protein kinase C 계열과 유사한 인산화 단백질임이 밝혀졌다. Streptomyces coelicolor is the best understood strain for the secondary-metabolits formation and cell differentiation among the Streptomyces. The afsR gene hed been cloned as a positive regulatory gene for the production of the secondary metabolites such as actinorhodin and undecylprodigiosin from Streptomyces coelicolor A3(2). The AfsR protein can be phosphorylated by a certain kinase (AfsK) which is located on the cell membrane and the phospho-relay system between the AfsR and AfsK is similar with the typical eukaryotic signal transduction system, The phosphorylated residues of the AfsR was very stable in extreme pH and solvent conditions. The protein kinase inhibitors, staurosporine and K-252a, showed severe inhibitory effect for the phophorylation of the AfsR protein and it was concluded the AfsR/AfsK phospho-relay system is similar with the eukaryotic protein kinase C family.
돈육 Oligopeptide를 첨가한 경구영양액의 품질특성
홍순광 ( Soon Kwang Hong ) 한국식품영양학회 2012 韓國食品營養學會誌 Vol.25 No.1
The objective of this study was to address the issues associated with the solubility of the pork meat oligopeptide, while maintaining its original nutritional value and improving its digestibility. The pork meat oligopeptide was used to produce an oral liquid supplement that was contained in a 200 ㎖can. The formulation was designed to satisfy 20% of the daily recommended nutrition intake of an adult male aged between 20 and 29. Analysis of the quality characteristics showed that this formulation was highly homogenized as an oral liquid supplement with advanced solubility. In addition, based on the viscosity, pH, color value, turbidity, and brix, the product was shown to advanced processing quality with great solubility; however, there was some concern that the taste would be deteriorated due to the bitter taste of the peptide. Thus, further studies need to be performed before this formulation can be commercialized.