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Biomedical subjects

S Liebe

Publications and source records attributed to S Liebe.

At least 109 records · Page 6Linked to original sources
PubMed1970

Hefe-phosphofructokinase: Reversible molekulare umwandlung und aufbau aus subeinheiten.

Yeast phosphofructokinase exists in several enzymically active, interconvertible forms with molecular weights of 180,000, 370,000, 570,000 and 750,000. With disc-electrophoresis catalytically active aggregation products with molecular weights of more than one million can be detected.In alkaline media fragmentation of phosphofructokinase occurs, leading to a variety of catalytically inactive products. These seem to be oligomers of subunits with 60,000 daltons. A model of the complex subunit structure of yeast phosphofructokinase is suggested. The various catalytically active forms of the enzyme are considered as polymers of 180,000 monomers, which themselves are enzymatically active and which are composed of three 60,000 subunits.

Journal Article↗
PubMed1970

Aggregationsformen der Rinderleberkatalase.

Bovine liver catalase is separated into several distinct bands by electrophoresis in a linear concentration gradient of polyacrylamide. Apparently, disc electrophoresis under these conditions leads to a series of enzymatic active forms of catalase. Their molecular weights are: 248,000; 295,000; 368,000; 486,000; 705,000 respectively. Density gradient centrifugation separates catalase into two components with molecular weights of 252,000 and 316,000. The observed differences in molecular weight distribution between gel-electrophoresis and density gradient centrifugation are discussed.

Journal Article↗