{"title":"慢性精神分裂症血清中多种形式单胺氧化酶的表征。","authors":"S A Al-Mudhaffar, N M Fahad","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Either half or one hour incubation time was enough to get a constant production of benzylaldehyde and were proportional to the amount of enzyme added. The optimal temperature of MAO, I, II, III, IV are 60 degrees, 37 degrees, 60 degrees, 45 degrees, and 37 degrees C respectively, and they follow Arrhenius equation until these optimal temperatures. Each form have optimal pH depends on substrate concentration used and the buffer used. These forms were shown to be inhibited by high substrate concentration with formation of inactive enzyme-amine complex, whereas butyl- and octylamine was found to be competitive inhibitors. Isoniazid inhibit MAO II, III, IV and V forms in a non competitive fashion, whereas MAO I inhibited competitively with respect to the substrate. Semicarbazid inhibit MAO I. III, IV and V forms in a non competitive fashion, whereas MAO II inhibited competitively with respect to the substrate.</p>","PeriodicalId":8818,"journal":{"name":"Biochemistry and experimental biology","volume":"15 4","pages":"317-27"},"PeriodicalIF":0.0000,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Characterization of the multiple forms of monoamine oxidase from chronic schizophrenic sera.\",\"authors\":\"S A Al-Mudhaffar, N M Fahad\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Either half or one hour incubation time was enough to get a constant production of benzylaldehyde and were proportional to the amount of enzyme added. The optimal temperature of MAO, I, II, III, IV are 60 degrees, 37 degrees, 60 degrees, 45 degrees, and 37 degrees C respectively, and they follow Arrhenius equation until these optimal temperatures. Each form have optimal pH depends on substrate concentration used and the buffer used. These forms were shown to be inhibited by high substrate concentration with formation of inactive enzyme-amine complex, whereas butyl- and octylamine was found to be competitive inhibitors. Isoniazid inhibit MAO II, III, IV and V forms in a non competitive fashion, whereas MAO I inhibited competitively with respect to the substrate. Semicarbazid inhibit MAO I. III, IV and V forms in a non competitive fashion, whereas MAO II inhibited competitively with respect to the substrate.</p>\",\"PeriodicalId\":8818,\"journal\":{\"name\":\"Biochemistry and experimental biology\",\"volume\":\"15 4\",\"pages\":\"317-27\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1979-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemistry and experimental biology\",\"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":"Biochemistry and experimental biology","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Characterization of the multiple forms of monoamine oxidase from chronic schizophrenic sera.
Either half or one hour incubation time was enough to get a constant production of benzylaldehyde and were proportional to the amount of enzyme added. The optimal temperature of MAO, I, II, III, IV are 60 degrees, 37 degrees, 60 degrees, 45 degrees, and 37 degrees C respectively, and they follow Arrhenius equation until these optimal temperatures. Each form have optimal pH depends on substrate concentration used and the buffer used. These forms were shown to be inhibited by high substrate concentration with formation of inactive enzyme-amine complex, whereas butyl- and octylamine was found to be competitive inhibitors. Isoniazid inhibit MAO II, III, IV and V forms in a non competitive fashion, whereas MAO I inhibited competitively with respect to the substrate. Semicarbazid inhibit MAO I. III, IV and V forms in a non competitive fashion, whereas MAO II inhibited competitively with respect to the substrate.