The radiation inactivation method allows determination of the relative molecular mass (M,) of proteins by exposure to high doses of ionizing radiation. The analysis by target theory of biological activity decay curves yields the size of the protein. A correction factor for M, has been routinely used
Temperature dependence of partial volumes of proteins
β Scribed by Henry B. Bull; Keith Breese
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1973
- Tongue
- English
- Weight
- 470 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
Abstract
The change of the apparent partial specific volumes of egg albumin, bovine serum albumin, bovine methemoglobin, Ξ²βlactoglobulin, and lysozyme with temperature through the thermal transitions of the proteins have been measured with dilatometers. Four regions in the plot of the apparent partial specific volumes against temperature can be recognized: (1) linear sections extending from 25Β°C up to 45β50Β°C: (2) a decrease in slope between 50Β°C and 60Β°C; (3) a sharp increase in slope with increasing temperature coinciding with the appearance of heat coagulation of the protein and followed by (4) a decrease in the slope. The return of the protein samples to 25Β°C yields linear relations between the apparent partial specific volumes of the heatβdenatured proteins and the decreasing temperature.
π SIMILAR VOLUMES
## Abstract The temperature dependence of the apparent expansibility of lysozyme and ovalbumin in Solution has been measured as a function of pH. This temperature dependence is explained in terms of suppressed fluctuations in bound water due to the protein. It is shown that the thermal expansion co
TABLE 1 ~ --.ct plutonium 4% Al 6 stabilized plutonium ~---\_--Time (hr) Slope ( 1O-s ,uw cm/hr) Normalised slope TSlope ( 1O-s ,uw cm/hr) Normalised slope -\_.