## Abstract Hydrodynamic studies of histone f2a1 are performed in dilute salt solution. Protein sedimentation is shown to be dependent upon the partial specific volume and molarity of the supporting electrolyte. To compensate for the secondary chage effect, a solvent of dilute tetramethylammonium c
A method for the differentiation of histone fractions F2(a)1 and F2(a)2 by starch gel electrophoresis
โ Scribed by E.W. Johns
- Publisher
- Elsevier Science
- Year
- 1968
- Tongue
- English
- Weight
- 682 KB
- Volume
- 34
- Category
- Article
- ISSN
- 1873-3778
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The reactions (1) ( 2 ) have been studied competitively over the range of 2%182'C by photolysis of mixtures of C12 + C2F5I + CH4. We obtain log k l / k 2 = (0.96 f 0.06) + (1210 f 440)/0 where 0 = 2.303RT J/mol. The use of published data on reaction (2) leads to log (kl(cms/mol sec) = (13.96 f 0.2)