Effect of Protein Chemical Hydrophobization on Antiglucose Oxidase Immunoglobulin Production in Mouse
: One problem resulting from the therapeutic use of enzymes is the adverse immunological reactions. In order to study the immunoglobulin production elicited into mice by different derivatives of an enzyme, glucose oxidase was chosen as a model. The immunoglobulin productions induced by apoglucose ox...
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Veröffentlicht in: | Pharmacology & toxicology 1995-04, Vol.76 (4), p.278-285 |
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description | : One problem resulting from the therapeutic use of enzymes is the adverse immunological reactions. In order to study the immunoglobulin production elicited into mice by different derivatives of an enzyme, glucose oxidase was chosen as a model. The immunoglobulin productions induced by apoglucose oxidase, prepared by removing flavine adenine dinucleotide from the native enzyme through an acidic treatment and devoid of enzymatic activity, by metaperiodate‐oxidized glucose oxidase that lost about 50% of its carbohydrate moiety, and by propyl aliphatic chains‐coupled glucose oxidase were as intense as that induced by native glucose oxidase. On the other hand, coupling hexyl aliphatic chains to the enzyme did change its ability to stimulate antibody production. This hydrophobized preparation induced a low titer of antibody after repeated intravenous or subcutaneous injections. This result suggests a simple strategy for reducing the immunogenicity of foreign proteins and for decreasing the risk of immunological complications in enzyme therapy. |
doi_str_mv | 10.1111/j.1600-0773.1995.tb00143.x |
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In order to study the immunoglobulin production elicited into mice by different derivatives of an enzyme, glucose oxidase was chosen as a model. The immunoglobulin productions induced by apoglucose oxidase, prepared by removing flavine adenine dinucleotide from the native enzyme through an acidic treatment and devoid of enzymatic activity, by metaperiodate‐oxidized glucose oxidase that lost about 50% of its carbohydrate moiety, and by propyl aliphatic chains‐coupled glucose oxidase were as intense as that induced by native glucose oxidase. On the other hand, coupling hexyl aliphatic chains to the enzyme did change its ability to stimulate antibody production. This hydrophobized preparation induced a low titer of antibody after repeated intravenous or subcutaneous injections. This result suggests a simple strategy for reducing the immunogenicity of foreign proteins and for decreasing the risk of immunological complications in enzyme therapy.</description><identifier>ISSN: 0901-9928</identifier><identifier>EISSN: 1600-0773</identifier><identifier>DOI: 10.1111/j.1600-0773.1995.tb00143.x</identifier><identifier>PMID: 7617559</identifier><identifier>CODEN: PHTOEH</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Apoenzymes - immunology ; Biological and medical sciences ; Electrophoresis, Polyacrylamide Gel ; Enzyme-Linked Immunosorbent Assay ; Female ; Flavin-Adenine Dinucleotide ; Glucose Oxidase - chemistry ; Glucose Oxidase - immunology ; Immunoglobulins - biosynthesis ; Medical sciences ; Mice ; Miscellaneous ; Oxidation-Reduction ; Periodic Acid - pharmacology ; Pharmacology. 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In order to study the immunoglobulin production elicited into mice by different derivatives of an enzyme, glucose oxidase was chosen as a model. The immunoglobulin productions induced by apoglucose oxidase, prepared by removing flavine adenine dinucleotide from the native enzyme through an acidic treatment and devoid of enzymatic activity, by metaperiodate‐oxidized glucose oxidase that lost about 50% of its carbohydrate moiety, and by propyl aliphatic chains‐coupled glucose oxidase were as intense as that induced by native glucose oxidase. On the other hand, coupling hexyl aliphatic chains to the enzyme did change its ability to stimulate antibody production. This hydrophobized preparation induced a low titer of antibody after repeated intravenous or subcutaneous injections. This result suggests a simple strategy for reducing the immunogenicity of foreign proteins and for decreasing the risk of immunological complications in enzyme therapy.</description><subject>Animals</subject><subject>Apoenzymes - immunology</subject><subject>Biological and medical sciences</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Female</subject><subject>Flavin-Adenine Dinucleotide</subject><subject>Glucose Oxidase - chemistry</subject><subject>Glucose Oxidase - immunology</subject><subject>Immunoglobulins - biosynthesis</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>Miscellaneous</subject><subject>Oxidation-Reduction</subject><subject>Periodic Acid - pharmacology</subject><subject>Pharmacology. Drug treatments</subject><subject>Protein Denaturation - drug effects</subject><subject>Structure-Activity Relationship</subject><issn>0901-9928</issn><issn>1600-0773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkF1L5DAUhsPiooP6ExaKiHetOabNhzeig1_gohfudUjzoZG2GZuWndlfb7pT5t4QOCec9z15eRA6AVxAOucfBVCMc8wYKUCIqhhqjKEkxfoHWuxGe2iBBYZciAt-gI5j9DUmFeMAJd1H-4wCqyqxQPbWOauHLLjspQ-D9V22fLet16rJHjamD6v3UPt_avChy9K97gb_1ow6RJs9r71RqT627diFtybUY5P8aY8Z9X9Dev0OY7RH6KdTTbTHcz1Ef-5uX5cP-dPz_ePy-inXRAiSC1crVnLumDIUFGhRAheUKzC4ZJQRoJqVUBknlKmxExeaY8Wwdgwbbhg5RGfbvas-fI42DrL1UdumUZ1NOSRLbswBJ-HlVqj7EGNvnVz1vlX9RgKWE2b5ISeWcmIpJ8xyxizXyfxr_mWsW2t21hlqmp_OcxUTR9erTvu4k5GS0opPYa-2sr--sZtvBJA3y5fX1JEvqGKa_g</recordid><startdate>199504</startdate><enddate>199504</enddate><creator>Shi, Qin</creator><creator>Domurado, Martine</creator><creator>Domurado, Dominique</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>199504</creationdate><title>Effect of Protein Chemical Hydrophobization on Antiglucose Oxidase Immunoglobulin Production in Mouse</title><author>Shi, Qin ; Domurado, Martine ; Domurado, Dominique</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3993-9fba7488f7ad61a1c9418968a1d04767316c7415df9adb0f92c80a70cf70d8d73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Animals</topic><topic>Apoenzymes - immunology</topic><topic>Biological and medical sciences</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Female</topic><topic>Flavin-Adenine Dinucleotide</topic><topic>Glucose Oxidase - chemistry</topic><topic>Glucose Oxidase - immunology</topic><topic>Immunoglobulins - biosynthesis</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>Miscellaneous</topic><topic>Oxidation-Reduction</topic><topic>Periodic Acid - pharmacology</topic><topic>Pharmacology. Drug treatments</topic><topic>Protein Denaturation - drug effects</topic><topic>Structure-Activity Relationship</topic><toplevel>online_resources</toplevel><creatorcontrib>Shi, Qin</creatorcontrib><creatorcontrib>Domurado, Martine</creatorcontrib><creatorcontrib>Domurado, Dominique</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Pharmacology & toxicology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shi, Qin</au><au>Domurado, Martine</au><au>Domurado, Dominique</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of Protein Chemical Hydrophobization on Antiglucose Oxidase Immunoglobulin Production in Mouse</atitle><jtitle>Pharmacology & toxicology</jtitle><addtitle>Pharmacol Toxicol</addtitle><date>1995-04</date><risdate>1995</risdate><volume>76</volume><issue>4</issue><spage>278</spage><epage>285</epage><pages>278-285</pages><issn>0901-9928</issn><eissn>1600-0773</eissn><coden>PHTOEH</coden><abstract>: One problem resulting from the therapeutic use of enzymes is the adverse immunological reactions. In order to study the immunoglobulin production elicited into mice by different derivatives of an enzyme, glucose oxidase was chosen as a model. The immunoglobulin productions induced by apoglucose oxidase, prepared by removing flavine adenine dinucleotide from the native enzyme through an acidic treatment and devoid of enzymatic activity, by metaperiodate‐oxidized glucose oxidase that lost about 50% of its carbohydrate moiety, and by propyl aliphatic chains‐coupled glucose oxidase were as intense as that induced by native glucose oxidase. On the other hand, coupling hexyl aliphatic chains to the enzyme did change its ability to stimulate antibody production. This hydrophobized preparation induced a low titer of antibody after repeated intravenous or subcutaneous injections. This result suggests a simple strategy for reducing the immunogenicity of foreign proteins and for decreasing the risk of immunological complications in enzyme therapy.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>7617559</pmid><doi>10.1111/j.1600-0773.1995.tb00143.x</doi><tpages>8</tpages></addata></record> |
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subjects | Animals Apoenzymes - immunology Biological and medical sciences Electrophoresis, Polyacrylamide Gel Enzyme-Linked Immunosorbent Assay Female Flavin-Adenine Dinucleotide Glucose Oxidase - chemistry Glucose Oxidase - immunology Immunoglobulins - biosynthesis Medical sciences Mice Miscellaneous Oxidation-Reduction Periodic Acid - pharmacology Pharmacology. Drug treatments Protein Denaturation - drug effects Structure-Activity Relationship |
title | Effect of Protein Chemical Hydrophobization on Antiglucose Oxidase Immunoglobulin Production in Mouse |
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