{"title":"[The aggregative stability of human oxyhemoglobin in aqueous media in the presence of mercury(II) compounds].","authors":"A E Myshkin","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>An analytical review of studies on human oxyhemoglobin coagulation has been performed by the author jointly with V. S. Koniaeva and L. D. Bogdanova within a period from 1985 to 1990. It was shown that the oxyhemoglobin coagulation modified by mercurials proceeded without any essential alteration of native protein conformation. A hypothesis is discussed that the oxyhemoglobin coagulation results from the primary polyaggregation of dimer fragments and that hydrophobic sites which provide for dimer-to-dimer contacts in native tetrameric oxyhemoglobin, participate in this process.</p>","PeriodicalId":14529,"journal":{"name":"Izvestiia Akademii nauk SSSR. Seriia biologicheskaia","volume":" 4","pages":"583-93"},"PeriodicalIF":0.0000,"publicationDate":"1991-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Izvestiia Akademii nauk SSSR. Seriia biologicheskaia","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
Abstract
An analytical review of studies on human oxyhemoglobin coagulation has been performed by the author jointly with V. S. Koniaeva and L. D. Bogdanova within a period from 1985 to 1990. It was shown that the oxyhemoglobin coagulation modified by mercurials proceeded without any essential alteration of native protein conformation. A hypothesis is discussed that the oxyhemoglobin coagulation results from the primary polyaggregation of dimer fragments and that hydrophobic sites which provide for dimer-to-dimer contacts in native tetrameric oxyhemoglobin, participate in this process.
作者与V. S. Koniaeva和L. D. Bogdanova共同对1985年至1990年期间关于人氧合血红蛋白凝固的研究进行了分析性回顾。结果表明,汞修饰的氧合血红蛋白凝血过程没有对天然蛋白构象产生任何本质的改变。讨论了一种假设,即氧血红蛋白凝固是由二聚体片段的初级多聚集引起的,而在天然四聚氧血红蛋白中提供二聚体到二聚体接触的疏水位点参与了这一过程。