{"title":"温度诱导的血清淀粉样蛋白SAA解离","authors":"R.P. Linke","doi":"10.1016/S0340-904X(79)80008-1","DOIUrl":null,"url":null,"abstract":"<div><p>Serum amyloid A protein (SAA) has been shown to be unstable at elevated temperatures. While in agreement with earlier reports, molecular weights of approximately 180,000 daltons were determined by gel filtration at 37°C and below, above 38°C additional AA-antigenic activity was found in the void volume and at the position of approximately 12,000 daltons. The latter polypeptide resembled in size and immunoreactivity SAAL in that it had AA-antigenic determinants exposed at 4°C (unlike SAA). Because the release of SAAL or a similar molecule could not be prevented by the enzyme inhibitor PMSF, a temperature-dependent dissociation of SAA is proposed.</p><p>In view of the known occurrence of amyloid following febrile conditions, the change in size and immunoreactivity of AA-antigenic proteins in vitro may indicate that a similar mechanism in vivo is important in the genesis of AA-type amyloidosis.</p></div>","PeriodicalId":101288,"journal":{"name":"Zeitschrift für Immunit?tsforschung: Immunobiology","volume":"155 3","pages":"Pages 255-261"},"PeriodicalIF":0.0000,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0340-904X(79)80008-1","citationCount":"4","resultStr":"{\"title\":\"Temperature-Induced Dissociation of Serum Amyloid Protein SAA\",\"authors\":\"R.P. Linke\",\"doi\":\"10.1016/S0340-904X(79)80008-1\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Serum amyloid A protein (SAA) has been shown to be unstable at elevated temperatures. While in agreement with earlier reports, molecular weights of approximately 180,000 daltons were determined by gel filtration at 37°C and below, above 38°C additional AA-antigenic activity was found in the void volume and at the position of approximately 12,000 daltons. The latter polypeptide resembled in size and immunoreactivity SAAL in that it had AA-antigenic determinants exposed at 4°C (unlike SAA). Because the release of SAAL or a similar molecule could not be prevented by the enzyme inhibitor PMSF, a temperature-dependent dissociation of SAA is proposed.</p><p>In view of the known occurrence of amyloid following febrile conditions, the change in size and immunoreactivity of AA-antigenic proteins in vitro may indicate that a similar mechanism in vivo is important in the genesis of AA-type amyloidosis.</p></div>\",\"PeriodicalId\":101288,\"journal\":{\"name\":\"Zeitschrift für Immunit?tsforschung: Immunobiology\",\"volume\":\"155 3\",\"pages\":\"Pages 255-261\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1979-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0340-904X(79)80008-1\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Zeitschrift für Immunit?tsforschung: Immunobiology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0340904X79800081\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Zeitschrift für Immunit?tsforschung: Immunobiology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0340904X79800081","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Temperature-Induced Dissociation of Serum Amyloid Protein SAA
Serum amyloid A protein (SAA) has been shown to be unstable at elevated temperatures. While in agreement with earlier reports, molecular weights of approximately 180,000 daltons were determined by gel filtration at 37°C and below, above 38°C additional AA-antigenic activity was found in the void volume and at the position of approximately 12,000 daltons. The latter polypeptide resembled in size and immunoreactivity SAAL in that it had AA-antigenic determinants exposed at 4°C (unlike SAA). Because the release of SAAL or a similar molecule could not be prevented by the enzyme inhibitor PMSF, a temperature-dependent dissociation of SAA is proposed.
In view of the known occurrence of amyloid following febrile conditions, the change in size and immunoreactivity of AA-antigenic proteins in vitro may indicate that a similar mechanism in vivo is important in the genesis of AA-type amyloidosis.