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Cellular Changes During Aging in Neural and Mesenchymal Tissues
Marshak, Daniel R. 한림대학교 한림과학원 부설 환경ㆍ생명과학연구소 1995 국제학술회의 Vol.1995 No.-
Among the afflictions of the elderly, many of the cruelest are degenerative neurological diseases that rob the individual of selected functions, leaving others intact. Tardive dyskinesia and other motor disorders resulting from Parkinsonism, amyotrophic lateral sclerosis, and Huntington's disease leave the patient mentally sound, but physically debilitated. In contrast to this, Alzheimer disease and related degenerative, neurological disorders find patients, particularly in the early stages of the ailment, physically able but suffering from increasing loss of memory, language, and emotional stability.
Characterization of DNA Topoisomerase II Using an Anti-Peptide Antibody
Lee, Kyung-Hee,Marshak, Daniel R.,Bae, Young-Seuk 생화학분자생물학회 1993 한국생화학회지 Vol.26 No.7
DNA topoisomerase II has been purified from bovine calf thymus nuclei using P4 phage knotted DNA as a substrate. The purified enzyme consists of two bands of molecular mass 170 and 160 kDa, as determined by sodium-dodecyl sulfate-polyacrylamide gel electrophoresis. The final product is dependent on ATP and $Mg^{2+}$, and is free of any nucleolytic, proteolytic, topoisomerase I, or protein kinase activity. A specific antibody against the amino terminal region (residues 34 to 51) of topoisomerase II has been developed. The specific antibody, designated BL1, reacts with both the 170 and 160 kDa bands of topoisomcrase II. The antibody BL1 does not affect topoisomerase II activity and the immunoprecipitates of topoisomerase II with BL1 have enzyme activity, suggesting that the 34 to 51 residues are not directly involved in the DNA binding, ATP-hydrolyzing, and DNA breaking-rejoining reactions of the enzyme. The immunoprecipitates can be used to assay topoisomerase II activity in crude extracts.
Characterization of DNA topoisomerase 2 Using an Anti - Peptide Antibody
Kyung Hee Lee,Daniel R . Marshak,Young Seuk Bae 생화학분자생물학회 1993 BMB Reports Vol.26 No.7
DNA topoisomerase Ⅱ has been purified from bovine calf thymus nuclei using P4 phage knotted DNA as a substrate. The purified enzyme consists of two bands of molecular mass 170 and 160 kDa, as determined by sodium-dodecyl sulfate-polyacrylamide gel electrophoresis. The final product is dependent on ATP and Mg^(2+), and is free of any nucleolytic, proteolytic, topoisomerase Ⅰ, or protein kinase activity. A specific antibody against the amino terminal region (residues 34 to 51) of topoisomerase Ⅱ has been developed. The specific antibody, designated BL1, reacts with both the 170 and 160 kDa bands of topoisomerase Ⅱ. The antibody BL1 does not affect topoisomerase Ⅱ activity and the immunoprecipitates of topoisomerase Ⅱ with BL1 have enzyme activity, suggesting that the 34 to 51 residues are not directly involved in the DNA binding, ATP-hydrolyzing, and DNA breaking-rejoining reactions of the enzyme. The immunoprecipitates can be used to assay topoisomerase Ⅱ activity in crude extracts.
강원도 지역에 서식하는 무당개구리에서 생물학적 활성을 지닌 Bombesin 유사 Peptide 에 관한 연구
박형진,이윤렬,권혁일,김일,유일재,D . R . Marshak ( Hyoung Jin Park,Yun Lyul Lee,Hyeok Yil Kwon,Yil Kim,Il Je Yu,Daniel r . Marshak ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.3
The present study was performed to purify a BLI from the skin of frogs, B. orientalis inhabiting Kangwon-Do, Korea, and then determine its physiological activities and amino acid sequence. A substance that shows bombesin-like immunoreactivity (BLI) was partially purified from crude methanol extract of the frog skin by using a column of alkaline alumina and Sephadex G-10. BLI was further purified by using RP C18 preparative HPLC in which BLI was separated into 5 peaks. The major peak (BLI-K1) containing 65% of total BLI was subjected to purify as a single component by using sequential HPLC of SP-ion exchange and RP C18. Content of BLI in each fraction was monitored by RIA for which bombesin antiserum with a high titer and affinity to BBS was raised in a guinea pig. Eventually, 890 ㎍ of BLI-K1 was homogeneously purified from 420g of the skin of B. orientalis and it was not differentiated from synthetic BBS in RP C18, gel permeation and SP-ion exchange HPLC. In the physiological activities, BLI-K1 was identical to synthetic BBS in stimulation of gastrin release and exocrine pancreatic secretion including volume, protein, bicarbonate, amylase and chymotrypsin output in anesthetized rats. Furthermore, molecular weight and partial amino acid sequence of BLI-K1 was revealed to be identical to synthetic BBS. Therefore, it is concluded from the above results that the skin of B. orientalis contains the same BBS that has been isolated from the skin of European Bombina.
Characterization of DNA Topoisomerase II Using an Anti-Peptide Antibody
Lee, Kyung Hee,Bae, Young Seuk,Marshak, Daniel R . 경북대학교 유전공학연구소 1995 遺傳工學硏究所報 Vol.10 No.1
DNA topoisomerase II has been purified from bovine calf thymus nuclei using P4 phage knotted DNA as a substrate. The purified enzyme consists of two bands of molecular mass 170 and 160 kDa, as determined by sodium-dodecyl sulfate-polyacrylamide gel electrophoresis. The final product is dependent on ATP and Mg^(2+), and is free of any nucleolytic, proteolytic, topoisomerase I, or protein kinase activity. A specific antibody against the amino terminal region (residues 34 to 51) of topoisomerase II has been developed. The specific antibody, designated BL1, reacts with both the 170 and 160 kDa bands of topoisomerase II. The antibody BL1 does not affect topoisomerase II activity and the immunoprecipitates of topoisomerase II with BL1 have enzyme activity, suggesting that the 34 to 51 residues are not directly involved in the DNA binding, ATP-hydrolyzing, and DNA breaking-rejoining reactions of the enzyme. The immunoprecipitates can be used to assay topoisomerase II activity in crude extracts.
Interaction of the β Subunit of Casein Kinase 2 with the Ribosomal Protein L5
Bae, Young Seuk,Kim, Jeong Min,Cha, Ji Young,Marshak, Daniel R . 경북대학교 유전공학연구소 1996 遺傳工學硏究所報 Vol.11 No.1
Casein kinase II (CKII) usually exists as a heterotetramer with α₂β₂, αα'β₂, or α'₂β₂. The α or α' subunits catalyze protein phosphorylation, whereas the function of the β subunit remains unclear. One of the possible functions of the β subunit may be to mediate the interaction of the catalytic subunit with target proteins. To identify proteins capable of associating with the β subunit in vivo, we have used a two-hybrid system. One protein identified is human ribosomal protein L5. The protein L5 does not interact with the α or α' subunits of CKII, supporting the idea that the β subunit can determine a substrate specificity of CKII. These results furthermore suggest a novel role for CKII in ribosomal L5 phosphorylation, in ribosomal assembly, or ribosomal transport in the intact cells. The protein L5 may act as a regulator of the activity or subcellular localization of CKII.
Kim, Jeong Min,Lee, Ji Hoon,Kim, Min Seung,Lee, Yim Tae,Bae, Young Seuk,Marshak, Daniel, R. 경북대학교 유전공학연구소 1997 遺傳工學硏究所報 Vol.12 No.1
Protein kinase CKII (CKII) is a heterotetramer composed of two catalytic (α or α') and two regulatory (β) subunits. Using the yeast two-hybrid system, we have identified the highly basic, ribosomal protein L41 as a cellular protein capable of interacting with the β subunit of CKII. We show, furthermore, using purified proteins, that L41 protein and CKIIβ associate directly in vitro. L41 protein is not a substrate for CKII phosphorylation, and it does not stimulate CKII activity with either β-casein or synthetic peptide substrate (RRREEETEEE). However, L41 protein stimulates the phosphorylation of DNA topoisomerase IIα by CKII by 2.5 times. Additionally, L41 protein enhances the autophosphorylation of CKIIα. The data indicate that L41 protein associates with CKII and can modulate its activity toward a specific substrate or substrates. The direct interaction of CKIIβ with ribosomal proteins also suggests that CKIIβ itself or CKII holoenzyme may be involved in ribosome assembly or translational control.