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        • KCI등재

          B형 간염바이러스 표면항원 검색을 위한 Latex agglutination 법에 대한 고찰

          허향숙 ( Hyang Suk Hur ),이경원 ( Kyng Won Lee ),양용석 ( Yong Suk Ryang ),송경순 ( Kyung Soon Song ),이삼열 ( Samuel Y. Lee ) 대한임상검사과학회 1985 대한임상검사과학회지(KJCLS) Vol.17 No.1

          The study subjects consisted of positive blood serum samples from 151 patients and negative blood serum samples from 56 patients referred for HBsAg test by ELISA in Yonsei University Yeong Dong Hospital during 5 month period from December, 1984 to April, 1985. HBs Ag was tested by latex agglutination, using the original (LA-A) method and the recently developed, modified (LA-B) method separately as well as RPHA. The results were as follows: 1. Of the 151 HBs Ag positive samples confirmed by ELISA, 140(92.7%) were confirmed positive by RPHA, 134(88.7%) by LA-A and 135(89.4%) by LA-B (P>0.05). 2. Of the 56 HBs Ag negative samples confirmed by ELISA 55(98.2%) were shown negative by RPHA, 53(94.6%) by LA-A and 52(92.9%) by LA-B (P>0.05). 3. Of the 142 moderate to strongly reactive samples (O.D>2.0) confirmed by ELISA, 139(97.9`` %) were confirmed positive by RPHA, 133(93.7%) by LA-B (P>0.05). Of the 9 weakly reactive samples (O.D<2.0) reported by ELISA, 1(1 1. 1%) each was shown positive by RPHA and LA-A and 2(22.2%) by LA-B (P>0.05). 4. Comparison of the original latex agglutination (LA-A) and the modified latex agglutination (LA-B) methods showed their predictability levels were 97.7% by LA-A and 97.1 % by LA-B. There was no significant statistical difference between the LA-A and LA-B methods(P>0.05) and a further advantage of the modified method is its economical use of reagents. On the basis mentioned above, we considered these techniques very useful detection methods because both LA-A and LA-B appear to be equivalent about predictability. Also they can be. applied for mass screening of HBs Ag, and as routine tests for private clinics and emergency testing of HBs Ag in blood banks.

        • KCI등재

          Cloning and Expression of Human Clotting Factor 9 cDNA in Escherichia coli

          Young-Won Lee(이영원),Hyang-Suk Hur(허향숙),Myoung-Hee Kim(김명희) 대한의생명과학회 1996 Biomedical Science Letters Vol.2 No.2

          인체 혈액 응고 9인자는 간에서 생성되며 461개의 아미노산으로 구성된 당단백질이다. 따라서 인체 혈액응고 9인자 cDNA를 찾기 위해 태아의 간(fetal liver) cDNA library를 PCR(Polymerase Chain reaction) 방법으로 screening 하였으며, 그 결과 ATG개시 코돈으로부터 TAA 종료 코돈까지 포함하는 1.4 kb의 9인자 cDNA를 찾았다. 또한 클론된 9인자 cDNA를 박데리아에서 발현시키기 위해 박테리아 발현 벡터인 pGEX-2T 플라스미드에 클로닝하므로써 pGEX-F9 플라스미드를 제조하였다. pGEX-F9로 형질전환된 E. coli에서 pGEX-F9의 발현을 유도하면 73 KDa 크기의 GST-factor9 융합 단백질이 다량 생성되며, 이 단백질이 혈액 응고 9인자 단백질을 함유하는 융합 단백질임을 혈액 응고 9인자 항체를 이용한 Western blot으로 입증하였다. E. coli에서 발현된 GST-factor 9 융합단백질은 전체 단백질의 약 20%를 차지하며, GST agarose bead를 이용한 one step purificarion 방법을 통해 GST-factor9 융합 단백질을 쉽게 분리할 수 있다. Human blood clotting (coagulation) factor 9 cDNA which codes for 461 amino acid has been cloned by screening human fetal liver cDNA library using PCR. This 1.4 kb cDNA spanning from the ATG initiation codon to the TAA termination codon was cloned into bacterial expression vector pGEX-2T, generating pGEX-F9 plasmid. The plasmid pGEX-F9 expresses about 73 kDa GST (Glutathione S-transferase)-Factor 9 fusion protein when introduced into E. coli. Western blot analysis using polyclonal antibody raised against human factor 9 confirmed this fusion protein contains factor 9 protein. The level of GST-factor 9 expression was about 20% of total protein and the purification of fusion protein was efficiently achieved by using GST agarose bead based on one step purification protocol.

        • KCI등재

          Cloning and Expression of Human Clotting Factor 9 cDNA in Escherichia coli

          Kim,Myoung-Hee,Hur,Hyang-Suk,Lee,Young-Won THE KOREAN SOCIETY FOR BIOMEDICAL LABORATORY SCIEN 1996 Journal of biomedical laboratory sciences Vol.2 No.2

          인체 혈액 응고 9인자는 간에서 생성되며 461개의 아미노산으로 구성된 당단백질이다. 따라서 인체 혈액응고 9인자 cDNA를 찾기 위해 태아의 간(fetal liver) cDNA library를 PCR(Polymerase Chain reaction) 방법으로 screening 하였으며, 그 결과 ATG개시 코돈으로부터 TAA 종료 코돈까지 포함하는 1.4 kb의 9인자 cDNA를 찾았다. 또한 클론된 9인자 cDNA를 박테리아에서 발현시키기 위해 박테리아 발현 벡터인 pGEX-2T 플라스미드에 클로닝하므로써 pGEX-F9 플라스미드를 제조하였다. pGEX-F9로 형질전환된 E. coli에서 pGEX-F9의 발현을 유도하면 73 kDa 크기의 GST-factor9 융합 단백질이 다량 생성되며, 이 단백질이 혈액 응고 9인자 단백질을 함유하는 융합 단백질임을 혈액 응고 9인자 항체를 이용한 Western bolt으로 입증하였다. E. coli에서 발현된 GST-factor 9 융합단백질은 전체 단백질의 약 20%를 차지하며, GST agarose bead를 이용한 one step purificarion 방법을 통해 GST-factor9 융합 단백질을 쉽게 분리할 수 있다. Human blood clotting (coagulation) factor 9 cDNA which codes for 461 amino acid has been cloned by screening human fetal liver cDNA library using PCR. This 1.4 kb cDNA spanning from the ATG initiation codon to the TAA termination codon was cloned into bacterial expression vector pGEX-2T, generating pGEX-F9 plasmid. The plasmid pGEX-F9 expresses about 73 kDa GST (Glutathione S-transferase)-Factor 9 fusion protein when introduced into E. coli. Western blot analysis using polyclonal antibody raised against human factor 9 confirmed this fusion protein contains factor 9 protein. The level of GST-factor 9 expression was about 20% of total protein and the purification of fusion protein was efficiently achieved by using GST agarose bead based on one step purification protocol.

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