D.R. Absolom , C.J. Van Oss , W. Zingg , A.W. Neumann
{"title":"蛋白质表面张力的测定2。血清白蛋白的表面张力,在蛋白质-空气界面处改变","authors":"D.R. Absolom , C.J. Van Oss , W. Zingg , A.W. Neumann","doi":"10.1016/0005-2795(81)90050-7","DOIUrl":null,"url":null,"abstract":"<div><p>Serum albumin, which itself has a surface tension of ⋍70.3 erg/cm<sup>2</sup>, when dissolved in water lowers the surface tension of water from 72.5 to ⋍50 erg/cm<sup>2</sup>, as measured by a variety of means, including the pendant drop, the Wilhelmy plate and the platinum ring methods. Equally low and even lower surface tensions are found with the contact angle method, on a thin layer of albumin that had been adsorbed onto a low energy surface and subsequently exposed to air. Surface tensions of drops of albumin solutions varying in concentration from 0.01 to 5.5% (w/v) yielded, with a contact angle method, values that only varied between 67 and 61 erg/cm<sup>2</sup>. With the pendant drop, the Wilhelmy plate and the platinum ring methods, one essentially measures the surface tension at the air-liquid interface, at which proteins tend to adsorb, and where reversible or irreversible reorientation can be expected. The same holds for a thin layer of protein adsorbed onto a low energy surface, exposed to air. Thus, when through the very act of surface tension measurement, or after adsorbing protein onto a substrate, protein is exposed at the air-liquid interface, it apparently loses the pronounced hydrophilicity characteristic of its native hydrated state and manifests through reorientation a much more hydrophobic tertiary configuration.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"670 1","pages":"Pages 74-78"},"PeriodicalIF":0.0000,"publicationDate":"1981-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90050-7","citationCount":"56","resultStr":"{\"title\":\"Determination of surface tensions of proteins II. Surface tension of serum albumin, altered at the protein-air interface\",\"authors\":\"D.R. Absolom , C.J. Van Oss , W. Zingg , A.W. Neumann\",\"doi\":\"10.1016/0005-2795(81)90050-7\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Serum albumin, which itself has a surface tension of ⋍70.3 erg/cm<sup>2</sup>, when dissolved in water lowers the surface tension of water from 72.5 to ⋍50 erg/cm<sup>2</sup>, as measured by a variety of means, including the pendant drop, the Wilhelmy plate and the platinum ring methods. Equally low and even lower surface tensions are found with the contact angle method, on a thin layer of albumin that had been adsorbed onto a low energy surface and subsequently exposed to air. Surface tensions of drops of albumin solutions varying in concentration from 0.01 to 5.5% (w/v) yielded, with a contact angle method, values that only varied between 67 and 61 erg/cm<sup>2</sup>. With the pendant drop, the Wilhelmy plate and the platinum ring methods, one essentially measures the surface tension at the air-liquid interface, at which proteins tend to adsorb, and where reversible or irreversible reorientation can be expected. The same holds for a thin layer of protein adsorbed onto a low energy surface, exposed to air. Thus, when through the very act of surface tension measurement, or after adsorbing protein onto a substrate, protein is exposed at the air-liquid interface, it apparently loses the pronounced hydrophilicity characteristic of its native hydrated state and manifests through reorientation a much more hydrophobic tertiary configuration.</p></div>\",\"PeriodicalId\":100165,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Protein Structure\",\"volume\":\"670 1\",\"pages\":\"Pages 74-78\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1981-08-28\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0005-2795(81)90050-7\",\"citationCount\":\"56\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Protein Structure\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0005279581900507\",\"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) - Protein Structure","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005279581900507","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Determination of surface tensions of proteins II. Surface tension of serum albumin, altered at the protein-air interface
Serum albumin, which itself has a surface tension of ⋍70.3 erg/cm2, when dissolved in water lowers the surface tension of water from 72.5 to ⋍50 erg/cm2, as measured by a variety of means, including the pendant drop, the Wilhelmy plate and the platinum ring methods. Equally low and even lower surface tensions are found with the contact angle method, on a thin layer of albumin that had been adsorbed onto a low energy surface and subsequently exposed to air. Surface tensions of drops of albumin solutions varying in concentration from 0.01 to 5.5% (w/v) yielded, with a contact angle method, values that only varied between 67 and 61 erg/cm2. With the pendant drop, the Wilhelmy plate and the platinum ring methods, one essentially measures the surface tension at the air-liquid interface, at which proteins tend to adsorb, and where reversible or irreversible reorientation can be expected. The same holds for a thin layer of protein adsorbed onto a low energy surface, exposed to air. Thus, when through the very act of surface tension measurement, or after adsorbing protein onto a substrate, protein is exposed at the air-liquid interface, it apparently loses the pronounced hydrophilicity characteristic of its native hydrated state and manifests through reorientation a much more hydrophobic tertiary configuration.