{"title":"牛胰腺凝乳蛋白酶原B定量评价及猪胰腺鉴定试验的新研究","authors":"M Charles","doi":"10.1016/0926-6569(64)90189-0","DOIUrl":null,"url":null,"abstract":"<div><p>In this work, bovine chymotrypsinogen B has been quantitatively determined and a first attempt has been made towards the identification of a chymotrypsinogen B in porcine pancreas.</p><p>The quantitative technique used for bovine chymotrypsinogen B involves acid denaturation of procarboxypeptidase A, separation of anionic from cationic proteins on CM-cellulose at pH 6.0 and determination of the activity of both fractions against acetyl-<span>l</span>-tyrosine ethylester after tryptic activation. By using the specific activity of the pure precursors, the weight ratio chymotrypsinogen A/chymotrypsinogen B is finally calculated. This ratio is shown to be about 4 in bovine pancreas and pancreatic juice.</p><p>The anionic proteins of porcine pancreas and pancreatic juice delay, as in the case of bovine pancreas a strong activity against acetyl-<span>l</span>-tyrosine ethylester. This kind of activity is not given by porcine procarboxypeptidase A which, in contrast with its bovine analog, does not hydrolyze acetyl-<span>l</span>-tyrosine ethylester after tryptic treatment, but my several other anionic proteins which can be partly separated on DEAE-cellulose at pH 8.0. It is not yet known whether or not one of these proteins is actually a chymotrypsinogen B.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 2","pages":"Pages 319-327"},"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)90189-0","citationCount":"6","resultStr":"{\"title\":\"Nouvelles recherches sur le chymotrypsinogène B evaluation quantitative dans le pancréas de boeuf et essai d'identification chez le porc\",\"authors\":\"M Charles\",\"doi\":\"10.1016/0926-6569(64)90189-0\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>In this work, bovine chymotrypsinogen B has been quantitatively determined and a first attempt has been made towards the identification of a chymotrypsinogen B in porcine pancreas.</p><p>The quantitative technique used for bovine chymotrypsinogen B involves acid denaturation of procarboxypeptidase A, separation of anionic from cationic proteins on CM-cellulose at pH 6.0 and determination of the activity of both fractions against acetyl-<span>l</span>-tyrosine ethylester after tryptic activation. By using the specific activity of the pure precursors, the weight ratio chymotrypsinogen A/chymotrypsinogen B is finally calculated. This ratio is shown to be about 4 in bovine pancreas and pancreatic juice.</p><p>The anionic proteins of porcine pancreas and pancreatic juice delay, as in the case of bovine pancreas a strong activity against acetyl-<span>l</span>-tyrosine ethylester. This kind of activity is not given by porcine procarboxypeptidase A which, in contrast with its bovine analog, does not hydrolyze acetyl-<span>l</span>-tyrosine ethylester after tryptic treatment, but my several other anionic proteins which can be partly separated on DEAE-cellulose at pH 8.0. It is not yet known whether or not one of these proteins is actually a chymotrypsinogen B.</p></div>\",\"PeriodicalId\":100170,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"volume\":\"92 2\",\"pages\":\"Pages 319-327\"},\"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)90189-0\",\"citationCount\":\"6\",\"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/0926656964901890\",\"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/0926656964901890","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Nouvelles recherches sur le chymotrypsinogène B evaluation quantitative dans le pancréas de boeuf et essai d'identification chez le porc
In this work, bovine chymotrypsinogen B has been quantitatively determined and a first attempt has been made towards the identification of a chymotrypsinogen B in porcine pancreas.
The quantitative technique used for bovine chymotrypsinogen B involves acid denaturation of procarboxypeptidase A, separation of anionic from cationic proteins on CM-cellulose at pH 6.0 and determination of the activity of both fractions against acetyl-l-tyrosine ethylester after tryptic activation. By using the specific activity of the pure precursors, the weight ratio chymotrypsinogen A/chymotrypsinogen B is finally calculated. This ratio is shown to be about 4 in bovine pancreas and pancreatic juice.
The anionic proteins of porcine pancreas and pancreatic juice delay, as in the case of bovine pancreas a strong activity against acetyl-l-tyrosine ethylester. This kind of activity is not given by porcine procarboxypeptidase A which, in contrast with its bovine analog, does not hydrolyze acetyl-l-tyrosine ethylester after tryptic treatment, but my several other anionic proteins which can be partly separated on DEAE-cellulose at pH 8.0. It is not yet known whether or not one of these proteins is actually a chymotrypsinogen B.