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Human RBCs blood group conversion from A to O using a novel α-N-acetylgalactosaminidase of high specific activity
α-N-acetylgalactosaminidase (αNAGA) can convert group A human red blood cells (RBCs) to group O. One novel αNAGA gene was cloned by PCR from Elizabethkingia meningosepticum Isolated from a domestic clinical sample. Pure recombinant αNAGA was obtained by genetic engineering and protein purification w...
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Published in: | Chinese science bulletin 2008-07, Vol.53 (13), p.2008-2016 |
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container_end_page | 2016 |
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creator | Yu, ChengYu Xu, Hua Wang, LiSheng Zhang, JianGeng Zhang, YangPei |
description | α-N-acetylgalactosaminidase (αNAGA) can convert group A human red blood cells (RBCs) to group O. One novel αNAGA gene was cloned by PCR from Elizabethkingia meningosepticum Isolated from a domestic clinical sample. Pure recombinant αNAGA was obtained by genetic engineering and protein purification with a calculated molecule of 49.6 kD. αNAGA was selective for terminal α-N-acetylgalacto- samine residue with a high specific activity, αNAGA could completely remove A antigens of 1 U (about 100 mL) group A1 or A2 RBCs in 1 h at pH 6.8 and 25℃ with s consumption of 1.5 or 0.4 mg recombinant enzyme. Enzyme-converted group A RBCs did not agglutinate after being mixed with monoclonal snti-A or sere of groups A, B, AB and O. Other blood group antigens except ABO had no change. FCM analysis showed that A antigens and A1 antigens disappeared while H antigens increased. It indicated that αNAGA successfully converted human blood group A RBCs to universally transfusable group O RBCs without the risk of ABO-incompaUble transfusion reactions. This αNAGA was suitable for producing universal RBCs to increase clinical transfusion safety, improve the RBCs supply, and to decrease transfusion cost and support transfusion service in case of emergency. |
doi_str_mv | 10.1007/s11434-008-0248-y |
format | article |
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One novel αNAGA gene was cloned by PCR from Elizabethkingia meningosepticum Isolated from a domestic clinical sample. Pure recombinant αNAGA was obtained by genetic engineering and protein purification with a calculated molecule of 49.6 kD. αNAGA was selective for terminal α-N-acetylgalacto- samine residue with a high specific activity, αNAGA could completely remove A antigens of 1 U (about 100 mL) group A1 or A2 RBCs in 1 h at pH 6.8 and 25℃ with s consumption of 1.5 or 0.4 mg recombinant enzyme. Enzyme-converted group A RBCs did not agglutinate after being mixed with monoclonal snti-A or sere of groups A, B, AB and O. Other blood group antigens except ABO had no change. FCM analysis showed that A antigens and A1 antigens disappeared while H antigens increased. It indicated that αNAGA successfully converted human blood group A RBCs to universally transfusable group O RBCs without the risk of ABO-incompaUble transfusion reactions. 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Sci. Bull</addtitle><addtitle>Chinese Science Bulletin</addtitle><description>α-N-acetylgalactosaminidase (αNAGA) can convert group A human red blood cells (RBCs) to group O. One novel αNAGA gene was cloned by PCR from Elizabethkingia meningosepticum Isolated from a domestic clinical sample. Pure recombinant αNAGA was obtained by genetic engineering and protein purification with a calculated molecule of 49.6 kD. αNAGA was selective for terminal α-N-acetylgalacto- samine residue with a high specific activity, αNAGA could completely remove A antigens of 1 U (about 100 mL) group A1 or A2 RBCs in 1 h at pH 6.8 and 25℃ with s consumption of 1.5 or 0.4 mg recombinant enzyme. Enzyme-converted group A RBCs did not agglutinate after being mixed with monoclonal snti-A or sere of groups A, B, AB and O. Other blood group antigens except ABO had no change. FCM analysis showed that A antigens and A1 antigens disappeared while H antigens increased. It indicated that αNAGA successfully converted human blood group A RBCs to universally transfusable group O RBCs without the risk of ABO-incompaUble transfusion reactions. This αNAGA was suitable for producing universal RBCs to increase clinical transfusion safety, improve the RBCs supply, and to decrease transfusion cost and support transfusion service in case of emergency.</description><subject>A抗原</subject><subject>Chemistry/Food Science</subject><subject>Earth Sciences</subject><subject>Engineering</subject><subject>Humanities and Social Sciences</subject><subject>Life Sciences</subject><subject>multidisciplinary</subject><subject>Physics</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>免疫反应</subject><subject>血型转换</subject><subject>输血反应</subject><issn>1001-6538</issn><issn>2095-9273</issn><issn>1861-9541</issn><issn>2095-9281</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><recordid>eNp9kM1OwzAMgCsEEmPwANwi7oGkaZP2OCZgSBOTEJyjLD9dRpuMpJ3Ux-JFeCYybWdOtmV_tvVl2S1G9xgh9hAxLkgBEaogyosKjmfZBFcUw7os8HnKEcKQlqS6zK5i3KaKYJZPsrAYOuHA--M8gnXrvQJN8MMOSO_2OkTrHTDBd2AGeg9WYIjWNUAA5_e6Bb8_8A0KqfuxbUQrZO-j6KyzSkQNvAEb22xA3GlpjZUg9e3e9uN1dmFEG_XNKU6zz-enj_kCLlcvr_PZEkqCyx4qKmohqaGFLFNUVY3qmmFptCKIKiWLQuSGlBSVjDLBFCuVVJjSglBMGCbTDB_3yuBjDNrwXbCdCCPHiB-k8aM0nqTxgzQ-JiY_MjHNukYHvvVDcOnNf6G706GNd8134vhayC9jW81zRlFOSEn-AP7VfQA</recordid><startdate>20080701</startdate><enddate>20080701</enddate><creator>Yu, ChengYu</creator><creator>Xu, Hua</creator><creator>Wang, LiSheng</creator><creator>Zhang, JianGeng</creator><creator>Zhang, YangPei</creator><general>SP Science in China Press</general><scope>2RA</scope><scope>92L</scope><scope>CQIGP</scope><scope>W91</scope><scope>~WA</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20080701</creationdate><title>Human RBCs blood group conversion from A to O using a novel α-N-acetylgalactosaminidase of high specific activity</title><author>Yu, ChengYu ; Xu, Hua ; Wang, LiSheng ; Zhang, JianGeng ; Zhang, YangPei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c315t-d6a9ac6f64c5ac6d8909971cfed306ddc44a2f35605767a7d75dcd16643613713</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>A抗原</topic><topic>Chemistry/Food Science</topic><topic>Earth Sciences</topic><topic>Engineering</topic><topic>Humanities and Social Sciences</topic><topic>Life Sciences</topic><topic>multidisciplinary</topic><topic>Physics</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>免疫反应</topic><topic>血型转换</topic><topic>输血反应</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yu, ChengYu</creatorcontrib><creatorcontrib>Xu, Hua</creatorcontrib><creatorcontrib>Wang, LiSheng</creatorcontrib><creatorcontrib>Zhang, JianGeng</creatorcontrib><creatorcontrib>Zhang, YangPei</creatorcontrib><collection>维普_期刊</collection><collection>中文科技期刊数据库-CALIS站点</collection><collection>维普中文期刊数据库</collection><collection>维普中文医药期刊数据库</collection><collection>中文科技期刊数据库- 镜像站点</collection><collection>CrossRef</collection><jtitle>Chinese science bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yu, ChengYu</au><au>Xu, Hua</au><au>Wang, LiSheng</au><au>Zhang, JianGeng</au><au>Zhang, YangPei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human RBCs blood group conversion from A to O using a novel α-N-acetylgalactosaminidase of high specific activity</atitle><jtitle>Chinese science bulletin</jtitle><stitle>Chin. Sci. Bull</stitle><addtitle>Chinese Science Bulletin</addtitle><date>2008-07-01</date><risdate>2008</risdate><volume>53</volume><issue>13</issue><spage>2008</spage><epage>2016</epage><pages>2008-2016</pages><issn>1001-6538</issn><issn>2095-9273</issn><eissn>1861-9541</eissn><eissn>2095-9281</eissn><abstract>α-N-acetylgalactosaminidase (αNAGA) can convert group A human red blood cells (RBCs) to group O. One novel αNAGA gene was cloned by PCR from Elizabethkingia meningosepticum Isolated from a domestic clinical sample. Pure recombinant αNAGA was obtained by genetic engineering and protein purification with a calculated molecule of 49.6 kD. αNAGA was selective for terminal α-N-acetylgalacto- samine residue with a high specific activity, αNAGA could completely remove A antigens of 1 U (about 100 mL) group A1 or A2 RBCs in 1 h at pH 6.8 and 25℃ with s consumption of 1.5 or 0.4 mg recombinant enzyme. Enzyme-converted group A RBCs did not agglutinate after being mixed with monoclonal snti-A or sere of groups A, B, AB and O. Other blood group antigens except ABO had no change. FCM analysis showed that A antigens and A1 antigens disappeared while H antigens increased. It indicated that αNAGA successfully converted human blood group A RBCs to universally transfusable group O RBCs without the risk of ABO-incompaUble transfusion reactions. This αNAGA was suitable for producing universal RBCs to increase clinical transfusion safety, improve the RBCs supply, and to decrease transfusion cost and support transfusion service in case of emergency.</abstract><cop>Heidelberg</cop><pub>SP Science in China Press</pub><doi>10.1007/s11434-008-0248-y</doi><tpages>9</tpages></addata></record> |
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subjects | A抗原 Chemistry/Food Science Earth Sciences Engineering Humanities and Social Sciences Life Sciences multidisciplinary Physics Science Science (multidisciplinary) 免疫反应 血型转换 输血反应 |
title | Human RBCs blood group conversion from A to O using a novel α-N-acetylgalactosaminidase of high specific activity |
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