Journal article
Studies on protein subunits II. Preparation and properties of active subunits of aldolase bound to a matrix
Abstract
Matrix-bound (MB) subunits of aldolase were prepared by attaching tetrameric aldolase to Sepharose and removing those subunits not covalently linked to Sepharose. Comparison of the protein contents of the MB-derivatives leads to the conclusion that under the conditions used, most molecules of aldolase were attached covalently via only one subunit. The properties of MB-subunit aldolase were compared with those of the corresponding matrix-bound …
Authors
Chan WW-C; Mawer HM
Journal
Archives of Biochemistry and Biophysics, Vol. 149, No. 1, pp. 136–145
Publisher
Elsevier
Publication Date
March 1972
DOI
10.1016/0003-9861(72)90307-4
ISSN
0003-9861
Fields of Research (FoR)
Medical Subject Headings (MeSH)
AnimalsCarboxypeptidasesChemical PhenomenaChemistryChemistry, PhysicalCyanogen BromideDrug StabilityFructose-Bisphosphate AldolaseFructosephosphatesHot TemperatureHydrogen-Ion ConcentrationIsoflurophateKineticsMacromolecular SubstancesMusclesPolysaccharidesProtein BindingProtein ConformationProtein DenaturationRabbitsTosyl CompoundsTrypsinUrea