{"id":3785,"date":"2024-05-01T16:18:53","date_gmt":"2024-05-01T08:18:53","guid":{"rendered":"\/chemistry\/?p=3785"},"modified":"2024-09-13T10:03:07","modified_gmt":"2024-09-13T02:03:07","slug":"%e8%8e%8a%e5%ad%90%e8%b6%85","status":"publish","type":"post","link":"\/chemistry\/?p=3785","title":{"rendered":"\u9673\u9298\u51f1(\u671f\u520a)"},"content":{"rendered":"\n<div class=\"wp-block-tkuwpbs5-bs5-container container chem_teach\" style=\"margin-top:var(--wp--preset--spacing--40);padding-top:var(--wp--preset--spacing--50);padding-bottom:var(--wp--preset--spacing--50);position:relative\" block_id=\"lq3fs6oyzthhmnpj8a\"><style><\/style>\n<div class=\"wp-block-tkuwpbs5-bs5-row row\">\n<h4 class=\"wp-block-heading\"><strong>\u4ee3\u8868\u6027\u8457\u4f5c<\/strong><\/h4>\n\n\n\n<h5 class=\"wp-block-heading\"><strong>I.&nbsp;\u671f\u520a\u8ad6\u6587(Referred papers)<\/strong><\/h5>\n\n\n\n<p>1. Chern, M.-K. &amp; Pietruszko, R., 1998 (Sep.1); Human aldehyde dehydrogenase E3 isozyme: the N-terminal primary structure. Biochem. J. 334: 487-488.<\/p>\n\n\n\n<p>2. Chern, M.-K. &amp; Pietruszko, R., 1999 (Jun.); Evidence for mitochondrial localization of betaine aldehyde dehydrogenase in rat liver-purification,characterization and comparison with human cytoplasmic E3 isozyme. Biochemistry and Cell Biology 77: 179-187.&nbsp;<\/p>\n\n\n\n<p>3. Ambroziak, W., Izaguirre, G., Abriola, D., Chern, M.-K., Pietruszko, R. 1999; Metabolism of retinaldehyde by human liver and kidney. Adv. Exp. Med. Biol. 463: 205-211.&nbsp;<\/p>\n\n\n\n<p>4. Chern, M.-K., Wu, T.-C., Hsieh, C.-H., Chou, C.-C., Liu, L.-F., Kuan, I.-C., Yeh, Y.-H., Hsiao, C.-D., Tam, M.F. 2000 (Jul. 28); Tyr115, Gln165 and Trp209 contribute to the 1, 2-epoxy-3- (p-nitrophenoxy)propane-conjugation activity of glutathione S-transferase cGSTM1-1. J. Mol. Biol. 300: 1257-1269.&nbsp;<\/p>\n\n\n\n<p>5. Chern, M.-K., Gage, D.A., Pietruszko, R. 2000 (Dec.); Betaine aldehyde, betaine, and choline levels in rat liver during ethanol metabolism. Biochem. Pharmacol. 60: 1629-1637.&nbsp;<\/p>\n\n\n\n<p>6. Pietruszko, R. and Chern, M.-K. 2001 (Jan.); Betaine aldehyde dehydrogenase from rat liver mitochondrial matrix. Chemico-biological interactions 130-132(1-3): 193-9.&nbsp;<\/p>\n\n\n\n<p>7. Chern MK, Chang KN, Liu LF, Tam TC, Liu YC, Liang YL, Tam MF. 2002 (May); Yeast ribosomal protein L12 is a substrate of protein arginine methyltransferase (RMT2). Journal of Biological Chemistry 277: 15345-15353.&nbsp;<\/p>\n\n\n\n<p>8. Wang, San-Lang, Chen,Yen-Hsu, Wang, Chuan-Lu, Yen, Yue-Horng, Chern, Ming-Kai. 2005 (Apr.); Purification and characterization of a serine protease extracellularly produced by Aspergillus fumigatus in a shrimp and crab shell powder medium Enzyme and Microbial Technology 36 : 660-665.&nbsp;<\/p>\n\n\n\n<p>9. Wang SL, Kao TY, Wang CL, Yen YH, Chern MK, Chen YH. 2006 (Aug.); A solvent stable metalloprotease produced by Bacillus sp. TKU004 and its application in the deproteinization of squid pen for beta-chitin preparation. Enzyme and Microbial Technology 39 :724-731.&nbsp;<\/p>\n\n\n\n<p>10. Tseng SF, Huang TW, Chen CW, Chern MK, Tam MF, Teng SC. 2006 (May); ShyA, a membrane protein for proper septation of hyphae in Streptomyces. Biochem Biophys Res Commun. 343:369-77.&nbsp;<\/p>\n\n\n\n<p>11. Chen YH , Chen WL, Wang YH, Huang MY and Chern MK. 2007 (Apr.); Spatiotemporal expression of zebrafish D- amino&nbsp;acid oxidase during early embryogenesis. Fish Physiol. Biochem. 33 : 73-80.&nbsp;<\/p>\n\n\n\n<p>12. Shih-Juei Wang, Chi-yang Yu, Cheng-Kang Lee, Ming-Kai Chern and I-Ching Kuan. 2008 (Aug.); Subunit fusion&nbsp;of two yeast D-amino acid oxidases enhances their thermostability and resistance to hydrogen peroxide. Biotechnology letters 30 : 1415-1422.&nbsp;<\/p>\n\n\n\n<p>13. Ming-Kai Chern*, Wei-Jyh Shiah, Jyun-Jie Chen , Tzung-You Tsai , Hsin-Yin Lin, Chien-Wei Liu (2009), Single-step protein purification by back flush in ion exchange&nbsp;chromatography, Analytical Biochemistry , 392: 174\u2013176.&nbsp;&nbsp;<\/p>\n\n\n\n<p>14. Hsin-Ying Lin, Sey-En Lin, Su-Fang Chien, Ming-Kai Chern* (2011), Electroporation for three commonly used yeast strains for two-hybrid screening experiments, Analytical Biochemistry, 416: 117-119, Epub 29 April 2011<\/p>\n\n\n\n<p>15. Ming-Kai Chern*,&nbsp; Huang-Yi Li, Po-Fan Chen,Su-Fang Chien* (2012), Taro \u03b1-galactosidase: A new gene product for blood conversion, Biocatalysis and Agricultural Biotechnology, 1: 135-139.<\/p>\n\n\n\n<p>16. Feng-ing Wang, Ming-kai Chern, Chi-wang Li, Min Yan, and Yu-hsien Hsieh (2012), Prevalence and antibiotic resistance of Listeria species in food products in Taipei, Taiwan, The African Journal of Microbiology Research, 6: 4702-4706.&nbsp;<\/p>\n\n\n\n<p>17. Jen-Hong Yen, Sheng-Fu Chen, Ming-Kai Chern, Po-Chien Lu* (2014), The effect of turbulent viscous shear stress on red blood cell hemolysis, J. Artif. Organs, 17:178-185.<\/p>\n\n\n\n<p>18. Jen-Hong Yen, Sheng-Fu Chen, Ming-Kai Chern, Po-Chien Lu* (2015), The effects of extensional stress on red blood cell hemolysis, Biomedical Engineering: Applications, Basis and Communications 27: 1550042 (11 pages)<\/p>\n<\/div>\n\n\n\n<div class=\"wp-block-tkuwpbs5-bs5-row row\">\n<h5 class=\"wp-block-heading\"><strong>II.&nbsp;\u7814\u8a0e\u6703\u8ad6\u6587(Conference papers)&nbsp;<\/strong><\/h5>\n\n\n\n<p>1. Wu, T.-C., Chern, M.-K., Hsieh, C.-H., Chou, C.-C., Liu, L.-F., Kuan, I.-C., Yeh, Y.-H., Hsiao,C.-D., Tam, M.F. 2000 (May); Struture of functional study of glutathione S-transferase cGSTM1-1 complexed with S-glutathione conjugated 1,2-epoxy-3-(p-nitrophenoxy) propane.&nbsp;\u7b2c\u516d\u5c46\u751f\u7269\u7269\u7406\u65b0\u77e5\u7814\u8a0e\u6703, No.S22, p.42,&nbsp;\u570b\u7acb\u6e05\u83ef\u5927\u5b78.<\/p>\n\n\n\n<p>2. Min-Kai Chern, Gin-Wen Cheng, Wen-Teish Chang, San-Lang Wang. 2004 (Oct.); Production of proteases from shellfish chitin wastes by Bacillus cereus Asia Pacific Confederation of Chemical Engineering (APCChE2004) , Kitakyushu , Japan.<\/p>\n\n\n\n<p>3. Ming-Chun Chiu, Tzung-You Tsai, Duan-Yue Hung, Ming-Kai Chern; Cloning, Homologous Expression, and Purification of ADH3 from Mitochondrial Matrix of the Yeast Saccahromyces cerivisiae. 2005 Annual Meeting of Chemical Society Located in Taipei; BC0400. 2005 (Nov.)<\/p>\n\n\n\n<p>4. Yi-Chih Tzeng, Ching-Yuan Mao, Ming-Kai Chern; Cloning, Expression, and Purification of Ald2p and Ald3p of the Yeast Saccharomyces cerevisiae. 2005 Annual Meeting of Chemical Society Located in Taipei; BC0401. 2005 (Nov.)<\/p>\n\n\n\n<p>5. Shu-Ping Wen, Kuo-Chen Chen, Hsin-Ying Lin, Tzung-You Tsai, I-Te Chen, Chih-Hsiung Cheng, Ming-Kai Chern; Yeast Two-hybrid Screening of YJR129C, a Putative Protein Methyltransferase Gene of the Yeast Saccharomyces cerevisiae. 2005 Annual Meeting of Chemical Society Located in Taipei; BC0403. 2005 (Nov.)<\/p>\n\n\n\n<p>6. Tzung-You Tsai, Ming-Kai Chern; Purification and Characterization of ALD4p from the Yeast Saccahromyces cerivisiae. 2006 Annual Meeting of Chemical Society Located in Taipei; B-057. 2006 (Nov.)<\/p>\n\n\n\n<p>7. Hsin-Ying Lin, Sey-En Lin, Ming-Kai Chern; Yeast Two-hybrid Screening of EBNA2 Interacting Proteins in the Human Lymphocyte cDNA Library.&nbsp;\u81fa\u5317\u91ab\u5b78\u5927\u5b7895\u5b78\u5e74\u5ea6\u5e2b\u751f\u806f\u5408\u5b78\u8853\u7814\u7a76\u767c\u8868\u6703\uff1bA-18. 2007 (May)<\/p>\n\n\n\n<p>8. Wei-Jyh Shiah , Yu-Chun Chen , Ming-Kai Chern. 2008 (Jul.); Non-degraded expression and one-step purification of yeast ALD6 enzyme in E. coli . The First International Symposium on Process Chemistry [ISPC 08] , Kyoto, Japan.<\/p>\n\n\n\n<p>9. Ming-Kai Chern, Yung-Yu Yang , How-Jing Lee; Characterization of a novel&nbsp;endonuclease of Drosophila retrotransposon and its application to the mosquito control. The 3rd International Symposium on Biological Control of Arthropods, Christchurch, ew Zealand; Session 4.2. 2009 (Feb.)<\/p>\n\n\n\n<p>10. Ming-Kai Chern (2010, Jun). An unexpected way out &#8211; protein purification by&nbsp;back flush in conventional chromatography. BioJohor 2010-The Second&nbsp;International Biotechnology and Biodiversity Conference, Johor Bahru, Malasia.<\/p>\n\n\n\n<p>11. Ming-Kai Chern (2010, Nov). A solvent stable metalloprotease produced by&nbsp;Bacillus sp. TKU004 and its application in the deproteinization of squid pen for beta-chitin preparation. The 2nd International and Cross-Strait Chitin and&nbsp;Chitosan Symposium , Qianjiang, Hubei, China.<\/p>\n\n\n\n<p>12. Hsin-Ying Lin and Ming-Kai Chern, A general protocol of improved transformation by electroporation for yeast two-hybrid screening experiment, 2011 Annual Yeast Meeting in Taiwan. Yang-Ming University, Taipei. 2011 (Sep.)<\/p>\n\n\n\n<p>13. Ming-Kai Chern; A One-plus-one Dimensional Gel Analysis for Identification of Protein Methylation in Yeast. The International Symposium on Science Research VNU University of Science 27-28 April 2015, Le Van Third Grand Lecture Hall, 19-Le Thanh Tong Str., Hoan Kiem Dist., Hanoi-Vietnam<\/p>\n\n\n\n<p>14. Ming-Kai Chern; Probability amplitude: from Feynman rules to the reciprocal relationship and the Born rule. Joint Symposium of Asia Five Universities, The 6th OPU-KIST-ECUST-TKU Joint Symposium &amp; The 5th OPU-TKU Joint Symposium &amp; The 3rd OPU-FZU Joint Symposium, November 9 (Thu) &#8211; 11 (Sat), 2017, Osaka Prefecture University, Sakai, Osaka, Japan<\/p>\n\n\n\n<p>15. Ming-Kai Chern; Screening of high efficiency fermenting yeast strains, The 7th ECUST-TKU-KIST-OPU on Advanced Materials and Their Applications November 1~3, 2018; East China University of Science and Technology, Yifu Building, Lecture Hall, Xuhui Campus, 130 Meilong Road, Xihui District, Shanghai, China<\/p>\n\n\n\n<p>16. Ming-Kai Chern; Cellular and Molecular Biology Laboratory, March 30, 2019, Kyoto\/Osaka-Taiwan International BNCT Conference at Osaka Medical College, Osaka, Japan<\/p>\n\n\n\n<p>17. Ming-Kai Chern;&nbsp;Yeast Two-hybrid Screening of EBNA2 Interacting Proteins in the Human Lymphocyte cDNA Library, The 7th HCMUT-TKU-OPUKMITL-DLU-TNU Joint Symposium on Chemistry, Environment, Natural Sciences and Technologies October 25, 2019 Ho Chi Minh City, Vietnam<\/p>\n<\/div>\n\n\n\n<div class=\"wp-block-tkuwpbs5-bs5-row row\">\n<h5 class=\"wp-block-heading\"><strong>III.&nbsp;\u5c08\u5229(Patent)<\/strong><\/h5>\n\n\n\n<p>1. \u86cb\u767d\u8cea\u7d14\u5316\u65b9\u6cd5&nbsp;(Method for Purifying Protein)\uff1a\u4e2d\u83ef\u6c11\u570b\/\u7b2cI 400128\u865f, Jul. 2013\uff1a\u7f8e\u570b\/\u7b2c8354511\u865f, Oct. 2012<\/p>\n\n\n\n<p>2. \u6c34\u6eb6\u6027\u5375\u6bbc\u819c\u7c89\u672b\u4e4b\u88fd\u5099\u65b9\u6cd5\uff1b\u4e2d\u83ef\u6c11\u570b\u5c08\u5229&nbsp;(I631951\uff0c2018\u901a\u904e)<\/p>\n\n\n\n<p>3. \u5fae\u91dd\u5143\u4ef6\u7684\u88fd\u9020\u65b9\u6cd5\u8207\u5fae\u91dd\u6a21\u5177\u7684\u88fd\u9020\u65b9\u6cd5\uff1a\u4e2d\u83ef\u6c11\u570b(\u767c\u660e\u7b2cI698263\u865f)\u548c\u65e5\u672c(\u7279\u8a31\u7b2c6731024\u53f7)\u5c08\u5229&nbsp;(2020 Jul.&nbsp;\u901a\u904e)<\/p>\n<\/div>\n\n\n\n<div class=\"wp-block-tkuwpbs5-bs5-row row\">\n<h5 class=\"wp-block-heading\"><strong>IV.&nbsp;\u8fd1\u671f\u53c3\u8207\u7814\u7a76\u8a08\u756b\uff1a<\/strong><\/h5>\n\n\n\n<p>1. 2016\/11\/01&nbsp;\u52e4\u5104\u86cb\u54c1\u79d1\u6280\u80a1\u4efd\u6709\u9650\u516c\u53f8&nbsp;&#8211;&nbsp;\u6c34\u6eb6\u6027\u5375\u6bbc\u819c\u4e4b\u88fd\u5099\u689d\u4ef6\u8207\u91cf\u7522\u7814\u7a76\u8a08\u756b&nbsp;(\u4e3b\u6301\u4eba)<\/p>\n\n\n\n<p>2. 2018\/09\/01&nbsp;\u5b5f\u9109\u751f\u5316\u79d1\u6280\u80a1\u4efd\u6709\u9650\u516c\u53f8&nbsp;&#8211;&nbsp;\u7121\u7db2\u5e03\u751f\u7269\u53ef\u5206\u89e3\u6c34\u51dd\u819c\u53ca\u6c34\u6eb6\u6027\u751f\u7269\u53ef\u5206\u89e3\u5948\u7c73\u7e96\u7dad\u6297\u83cc\u6577\u6750&nbsp;(\u4e3b\u6301\u4eba)<\/p>\n\n\n\n<p>3. 2019\/08\/01&nbsp;\u6b23\u6897\u79d1\u6280\u80a1\u4efd\u6709\u9650\u516c\u53f8&nbsp;&#8211;&nbsp;\u7522\u54c1\u6e2c\u8a66\u8a08\u756b&nbsp;(\u4e3b\u6301\u4eba)<\/p>\n\n\n\n<p>4. 2020\/06\/01&nbsp;\u7522\u5b78\u5408\u4f5c\u8a08\u756b(\u5b5f\u9109\u751f\u5316\u79d1\u6280\u80a1\u4efd\u6709\u9650\u516c\u53f8) -\u5ba2\u88fd\u5316\u7f8e\u5bb9\u5fae\u91dd\u88fd\u7a0b&nbsp;(\u5171\u540c\u4e3b\u6301\u4eba)<\/p>\n<\/div>\n<\/div>\n\n\n\n<div style=\"height:10px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n","protected":false},"excerpt":{"rendered":"","protected":false},"author":21,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"wp-custom-template-member-empty-template","format":"standard","meta":{"footnotes":""},"categories":[1],"tags":[],"acf":[],"_links":{"self":[{"href":"\/chemistry\/index.php?rest_route=\/wp\/v2\/posts\/3785"}],"collection":[{"href":"\/chemistry\/index.php?rest_route=\/wp\/v2\/posts"}],"about":[{"href":"\/chemistry\/index.php?rest_route=\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"\/chemistry\/index.php?rest_route=\/wp\/v2\/users\/21"}],"replies":[{"embeddable":true,"href":"\/chemistry\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=3785"}],"version-history":[{"count":5,"href":"\/chemistry\/index.php?rest_route=\/wp\/v2\/posts\/3785\/revisions"}],"predecessor-version":[{"id":5730,"href":"\/chemistry\/index.php?rest_route=\/wp\/v2\/posts\/3785\/revisions\/5730"}],"wp:attachment":[{"href":"\/chemistry\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=3785"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"\/chemistry\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=3785"},{"taxonomy":"post_tag","embeddable":true,"href":"\/chemistry\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=3785"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}