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Aldehyde dehydrogenase from bovine liver has been purified to homogeneity. Amino acid composition showed a high content of cysteine of 32 mol/mol enzyme. The enzyme is composed of four identical subunits as judged by sodium dodecyl sulfate gel electrophoresis and end‐group analysis. The molecular weight was determined to be 220 000 ± 10 000 by sedimentation equilibrium analysis in an analytical ultracentrifuge. The Michaelis constants for NAD+, glyceraldehyde and acetaldehyde were found to be 47 μM, 170 μM and 130 μM, respectively.

1. Phosphoglycerate kinase was purified in homogeneous form from bovine kidney. 2. The molecular weight was found to be 49000 from amino acid composition and ultracentrifugation studies. 3. The pH optima for the phosphorylation of ADP was 8.0, and for the phosphorylation of 3-phosphoglycerate, 7.3. 4. The Michaelis constants at pH 8.25 for 3-phosphoglyceroyl phosphate and ADP were estimated to be 0.083 and 0.2mM respectively; 3-phosphogly- Phosphoglycerat-Kinase aus NierenZusammenfassung: l. Phosphoglycerat-Kinase wurde in homogener Form aus der Niere vom Rind isoliert. 2. Aus der Aminosäurezusammensetzung und auf der analytischen Ultrazentrifuge wurde ein Molekulargewicht von 49000 gefunden. 3. Das pH-Optimum für die Phosphorylierung von ADP war 8.0 und für die Phosphorylierung von 3-Phosphoglycerat 7.3. 4. Die Michaelis-Konstanten wurden bei pH 8.25 für 3-Phosphoglyceroylphosphat zu 0.083 und für ADP zu 0.2mM bestimmt. 3-Phosphoglycerat cerate acts as a competitive inhibitor with respect to 3-phosphoglyceroyl phosphate (Ki = 1.3mM). AtpH7.3, aATmvalueof0.15mMwasfoundforADP.

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