Y Kita, M F Rohde, T Arakawa, K D Fagin, E N Fish, K Banerjee
{"title":"重组人干扰素- γ聚乙二醇偶联物的表征。","authors":"Y Kita, M F Rohde, T Arakawa, K D Fagin, E N Fish, K Banerjee","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Recombinant human interferon-gamma was conjugated with polyethylene glycol (PEG) using succinimidyl coupling of amino groups in the protein. The PEG conjugated material showed antiviral, growth inhibitory and macrophage activation activities indistinguishable from those of the unmodified protein. The PEG conjugation reduced the receptor binding affinity slightly, but increased the half-life of the protein when measured in rats. Almost no clearance was observed within 6 hr after injection for the PEG conjugated protein, whereas a rapid clearance was seen for the unmodified interferon-gamma. Two possible sites of PEG attachment were identified in the protein: the N-terminal amino group and either lysine 129 or 131.</p>","PeriodicalId":11271,"journal":{"name":"Drug design and delivery","volume":"6 3","pages":"157-67"},"PeriodicalIF":0.0000,"publicationDate":"1990-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Characterization of a polyethylene glycol conjugate of recombinant human interferon-gamma.\",\"authors\":\"Y Kita, M F Rohde, T Arakawa, K D Fagin, E N Fish, K Banerjee\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Recombinant human interferon-gamma was conjugated with polyethylene glycol (PEG) using succinimidyl coupling of amino groups in the protein. The PEG conjugated material showed antiviral, growth inhibitory and macrophage activation activities indistinguishable from those of the unmodified protein. The PEG conjugation reduced the receptor binding affinity slightly, but increased the half-life of the protein when measured in rats. Almost no clearance was observed within 6 hr after injection for the PEG conjugated protein, whereas a rapid clearance was seen for the unmodified interferon-gamma. Two possible sites of PEG attachment were identified in the protein: the N-terminal amino group and either lysine 129 or 131.</p>\",\"PeriodicalId\":11271,\"journal\":{\"name\":\"Drug design and delivery\",\"volume\":\"6 3\",\"pages\":\"157-67\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1990-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Drug design and delivery\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Drug design and delivery","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Characterization of a polyethylene glycol conjugate of recombinant human interferon-gamma.
Recombinant human interferon-gamma was conjugated with polyethylene glycol (PEG) using succinimidyl coupling of amino groups in the protein. The PEG conjugated material showed antiviral, growth inhibitory and macrophage activation activities indistinguishable from those of the unmodified protein. The PEG conjugation reduced the receptor binding affinity slightly, but increased the half-life of the protein when measured in rats. Almost no clearance was observed within 6 hr after injection for the PEG conjugated protein, whereas a rapid clearance was seen for the unmodified interferon-gamma. Two possible sites of PEG attachment were identified in the protein: the N-terminal amino group and either lysine 129 or 131.