Arlene Krehbiel , Beatrice Kassell, M. Laskowski Sr.
{"title":"凝乳胰蛋白酶原B的活化","authors":"Arlene Krehbiel , Beatrice Kassell, M. Laskowski Sr.","doi":"10.1016/0926-6569(64)90188-9","DOIUrl":null,"url":null,"abstract":"<div><p>During the process of activation of chymotrypsinogen B at least 3 stages of activity levels can be distinguished. The first is the least stable, the third the most stable. With the same concentration of enzyme precursors and activating trypsin (EC 3.4.4.4) the initial rate of formation of chymotrypsin B (EC 3.4.4.6) is about 25 times higher than that of α-chymotrypsin (EC 3.4.4.5). With a constant time and varied concentration of trypsin, chymotrypsinogen B reaches a maximum activity level with one-tenth the amount of trypsin required to reach a maximum activity for α-chymotrypsinogen. The first activating cleavage is the same in both enzyme precursors and involves the bond arginine-isoleucine.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 2","pages":"Pages 312-318"},"PeriodicalIF":0.0000,"publicationDate":"1964-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90188-9","citationCount":"4","resultStr":"{\"title\":\"Activation of chymotrypsinogen B\",\"authors\":\"Arlene Krehbiel , Beatrice Kassell, M. Laskowski Sr.\",\"doi\":\"10.1016/0926-6569(64)90188-9\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>During the process of activation of chymotrypsinogen B at least 3 stages of activity levels can be distinguished. The first is the least stable, the third the most stable. With the same concentration of enzyme precursors and activating trypsin (EC 3.4.4.4) the initial rate of formation of chymotrypsin B (EC 3.4.4.6) is about 25 times higher than that of α-chymotrypsin (EC 3.4.4.5). With a constant time and varied concentration of trypsin, chymotrypsinogen B reaches a maximum activity level with one-tenth the amount of trypsin required to reach a maximum activity for α-chymotrypsinogen. The first activating cleavage is the same in both enzyme precursors and involves the bond arginine-isoleucine.</p></div>\",\"PeriodicalId\":100170,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"volume\":\"92 2\",\"pages\":\"Pages 312-318\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-11-22\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6569(64)90188-9\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926656964901889\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926656964901889","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
During the process of activation of chymotrypsinogen B at least 3 stages of activity levels can be distinguished. The first is the least stable, the third the most stable. With the same concentration of enzyme precursors and activating trypsin (EC 3.4.4.4) the initial rate of formation of chymotrypsin B (EC 3.4.4.6) is about 25 times higher than that of α-chymotrypsin (EC 3.4.4.5). With a constant time and varied concentration of trypsin, chymotrypsinogen B reaches a maximum activity level with one-tenth the amount of trypsin required to reach a maximum activity for α-chymotrypsinogen. The first activating cleavage is the same in both enzyme precursors and involves the bond arginine-isoleucine.
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