{"title":"[人血单个核细胞群中的氨基肽酶活性]。","authors":"D Kunz, E Schön, H J Hütter, S Ansorge","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The aminopeptidase N (AP N, EC 3.4.11.2) is an ectoenzyme of the plasma membrane, playing presumably an important role in the regulation of immunological processes. The specific activities of Ala-pNA and Leu-pNA cleavage (per cell) are distributed in monocytes T- and non-T-lymphocytes in a proportion of 1:0.2:0.25 and 1:0.17:0.18, respectively. The capacities of Ala-pNA and Leu-pNA hydrolysis in the total fraction T- and non-T-cells are distributed as 1:0.8 and 1:0.7, respectively. The main part of Ala-pNA cleavage was shown to be caused by AP N on the basis of the KM-value (0.5 mmol/l), the activation by CO2+ ions and the pH optimum (7.0-7.5). The Leu-pNA cleavage is dependent on CO2+ and DTT and distinct from the classical cytosolic leucyl aminopeptidase.</p>","PeriodicalId":7505,"journal":{"name":"Allergie und Immunologie","volume":"36 4","pages":"233-43"},"PeriodicalIF":0.0000,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Aminopeptidase activity in populations of human blood mononuclear cells].\",\"authors\":\"D Kunz, E Schön, H J Hütter, S Ansorge\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The aminopeptidase N (AP N, EC 3.4.11.2) is an ectoenzyme of the plasma membrane, playing presumably an important role in the regulation of immunological processes. The specific activities of Ala-pNA and Leu-pNA cleavage (per cell) are distributed in monocytes T- and non-T-lymphocytes in a proportion of 1:0.2:0.25 and 1:0.17:0.18, respectively. The capacities of Ala-pNA and Leu-pNA hydrolysis in the total fraction T- and non-T-cells are distributed as 1:0.8 and 1:0.7, respectively. The main part of Ala-pNA cleavage was shown to be caused by AP N on the basis of the KM-value (0.5 mmol/l), the activation by CO2+ ions and the pH optimum (7.0-7.5). The Leu-pNA cleavage is dependent on CO2+ and DTT and distinct from the classical cytosolic leucyl aminopeptidase.</p>\",\"PeriodicalId\":7505,\"journal\":{\"name\":\"Allergie und Immunologie\",\"volume\":\"36 4\",\"pages\":\"233-43\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1990-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Allergie und Immunologie\",\"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":"Allergie und Immunologie","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
氨基肽酶N (AP N, EC 3.4.11.2)是一种质膜外酶,可能在免疫过程的调节中起重要作用。Ala-pNA和Leu-pNA切割的特异性活性(每细胞)在单核细胞T淋巴细胞和非T淋巴细胞中分别以1:0.2:0.25和1:0.17:0.18的比例分布。Ala-pNA和Leu-pNA在T细胞和非T细胞总分数中的水解能力分别为1:0.8和1:7 .7。基于km值(0.5 mmol/l)、CO2+离子活化和最适pH值(7.0 ~ 7.5),表明AP N是Ala-pNA断裂的主要原因。Leu-pNA的分裂依赖于CO2+和DTT,不同于经典的细胞质亮氨酸氨基肽酶。
[Aminopeptidase activity in populations of human blood mononuclear cells].
The aminopeptidase N (AP N, EC 3.4.11.2) is an ectoenzyme of the plasma membrane, playing presumably an important role in the regulation of immunological processes. The specific activities of Ala-pNA and Leu-pNA cleavage (per cell) are distributed in monocytes T- and non-T-lymphocytes in a proportion of 1:0.2:0.25 and 1:0.17:0.18, respectively. The capacities of Ala-pNA and Leu-pNA hydrolysis in the total fraction T- and non-T-cells are distributed as 1:0.8 and 1:0.7, respectively. The main part of Ala-pNA cleavage was shown to be caused by AP N on the basis of the KM-value (0.5 mmol/l), the activation by CO2+ ions and the pH optimum (7.0-7.5). The Leu-pNA cleavage is dependent on CO2+ and DTT and distinct from the classical cytosolic leucyl aminopeptidase.