In:
European Journal of Biochemistry, Wiley, Vol. 38, No. 3 ( 1973-10), p. 479-488
Kurzfassung:
A new and efficient method for preparation of pure yeast phosphofructokinase is described, leading rapidly to an enzyme with minimum proteolytic alterations. Essential is an affinity chromatography step on the reactive dye Cibacron blue F3G‐A® which has been covalently bound to Sephadex G‐100. The enzyme prepared by this method has a significantly higher sedimentation constant (20.5 S) than those forms of yeast phosphofructokinase purified by procedures previously described (17.8 S) and is composed of two different kinds of subunits having molecular weights of 130000 and 96000, respectively. By gel filtration various enzyme fractions have been obtained, containing either mainly subunits of the 130000 or of the 96000 type, respectively. Samples of phosphofructokinase which have been prepared by the original and by the new method were compared by means of analytical gel chromatography and dodecyl‐sulphate electrophoresis. In the course of the preparation procedure described previously, the enzyme is evidently proteolytically converted to the 570000 molecule by degradation of the subunits having 130000 molecular weight to those of 96000.
Materialart:
Online-Ressource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1973.38.issue-3
DOI:
10.1111/j.1432-1033.1973.tb03083.x
Sprache:
Englisch
Verlag:
Wiley
Publikationsdatum:
1973
ZDB Id:
1398347-7
ZDB Id:
2172518-4
SSG:
12
Permalink