590. On detergent-protein interactions

E. D. Goddard; B. A. Pethica

doi:10.1039/JR9510002659

590. On detergent-protein interactions

E. D. Goddard, B. A. Pethica

Chemical & Biological Engineering

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Abstract

Calorimetric measurements of the heat of interaction of sodium dodecyl sulphate and bovine serum albumin have been carried out on both sides of the isoelectric point. The results have been interpreted in terms of previously reported stoicheiometric complexes. The heat data are compared with the theoretical calculations of the heats of binding.

Original language	English (US)
Pages (from-to)	2659-2663
Number of pages	5
Journal	Journal of the Chemical Society (Resumed)
DOIs	https://doi.org/10.1039/JR9510002659
State	Published - 1951

All Science Journal Classification (ASJC) codes

General Chemistry

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10.1039/JR9510002659

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title = "590. On detergent-protein interactions",

abstract = "Calorimetric measurements of the heat of interaction of sodium dodecyl sulphate and bovine serum albumin have been carried out on both sides of the isoelectric point. The results have been interpreted in terms of previously reported stoicheiometric complexes. The heat data are compared with the theoretical calculations of the heats of binding.",

author = "Goddard, {E. D.} and Pethica, {B. A.}",

year = "1951",

doi = "10.1039/JR9510002659",

language = "English (US)",

pages = "2659--2663",

journal = "Journal of the Chemical Society (Resumed)",

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AU - Goddard, E. D.

AU - Pethica, B. A.

PY - 1951

Y1 - 1951

N2 - Calorimetric measurements of the heat of interaction of sodium dodecyl sulphate and bovine serum albumin have been carried out on both sides of the isoelectric point. The results have been interpreted in terms of previously reported stoicheiometric complexes. The heat data are compared with the theoretical calculations of the heats of binding.

AB - Calorimetric measurements of the heat of interaction of sodium dodecyl sulphate and bovine serum albumin have been carried out on both sides of the isoelectric point. The results have been interpreted in terms of previously reported stoicheiometric complexes. The heat data are compared with the theoretical calculations of the heats of binding.

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U2 - 10.1039/JR9510002659

DO - 10.1039/JR9510002659

M3 - Article

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EP - 2663

JO - Journal of the Chemical Society (Resumed)

JF - Journal of the Chemical Society (Resumed)

ER -

590. On detergent-protein interactions

Abstract

All Science Journal Classification (ASJC) codes

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