{"title":"[纤维蛋白原分子的生物活性低分子片段]。","authors":"A O Musialkivs'ka, T M Platonova, Iu L Radavs'kiĭ","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>A peptide fraction with a specific property of interaction with D fragment was found in the fibrinogen tryptic hydrolyzate. This fraction is called a protector. In the protector presence the time of the monomer fibrin polymerization prolonged with D fragment is greatly lowered. The protector was found in the first minutes of fibrinogen degradation. It was shown for low concentration of trypsin (enzyme-substrate ratio being 1:7500). The gel filtration of a tryptic fibrinogen hydrolyzate on Sephadexes G-10, G-15, G-25 showed that the protector has a low molecular weight. It was found that a preincubation of the protector with D fragment should take place before interaction of their mixture with a fibrin monomer. The interaction of the protector with D fragment is reversible.</p>","PeriodicalId":23396,"journal":{"name":"Ukrains'kyi biokhimichnyi zhurnal","volume":"49 3","pages":"89-93"},"PeriodicalIF":0.0000,"publicationDate":"1977-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Biologically active low-molecular fragments of fibrinogen molecule].\",\"authors\":\"A O Musialkivs'ka, T M Platonova, Iu L Radavs'kiĭ\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A peptide fraction with a specific property of interaction with D fragment was found in the fibrinogen tryptic hydrolyzate. This fraction is called a protector. In the protector presence the time of the monomer fibrin polymerization prolonged with D fragment is greatly lowered. The protector was found in the first minutes of fibrinogen degradation. It was shown for low concentration of trypsin (enzyme-substrate ratio being 1:7500). The gel filtration of a tryptic fibrinogen hydrolyzate on Sephadexes G-10, G-15, G-25 showed that the protector has a low molecular weight. It was found that a preincubation of the protector with D fragment should take place before interaction of their mixture with a fibrin monomer. The interaction of the protector with D fragment is reversible.</p>\",\"PeriodicalId\":23396,\"journal\":{\"name\":\"Ukrains'kyi biokhimichnyi zhurnal\",\"volume\":\"49 3\",\"pages\":\"89-93\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1977-05-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Ukrains'kyi biokhimichnyi zhurnal\",\"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":"Ukrains'kyi biokhimichnyi zhurnal","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[Biologically active low-molecular fragments of fibrinogen molecule].
A peptide fraction with a specific property of interaction with D fragment was found in the fibrinogen tryptic hydrolyzate. This fraction is called a protector. In the protector presence the time of the monomer fibrin polymerization prolonged with D fragment is greatly lowered. The protector was found in the first minutes of fibrinogen degradation. It was shown for low concentration of trypsin (enzyme-substrate ratio being 1:7500). The gel filtration of a tryptic fibrinogen hydrolyzate on Sephadexes G-10, G-15, G-25 showed that the protector has a low molecular weight. It was found that a preincubation of the protector with D fragment should take place before interaction of their mixture with a fibrin monomer. The interaction of the protector with D fragment is reversible.