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Seed germination studies. I. Purification and properties of an alpha-amylase from the cotyledons of germinating peas.
A starch-hydrolyzing enzyme present in extracts of the cotyledons of germinating peas has been purified over 3400-fold and is similar in action pattern to other known plant α-amylases. Expand
Positive interference with the Jaffé reaction by cephalosporin antibiotics.
It does not appear possible to avoid the cephalosporin-caused interference by the use of "kinetic" creatinine methods, and several structurally similar compounds do not react under these same conditions. Expand
Seed germination studies. II. Pathways for starch degradation in germinating pea seedlings.
Amylase activity is present in extracts of the axis tissue of etiolated pea seedlings and it is established that this starch-hydrolyzing activity is due to the presence of a β-amylase (α-1,4-glucan maltohydrolase, EC; the properties of this enzyme are reported. Expand
Inhibition of protein synthesis in cell-free systems by homocitrullylamino adenosine
Abstract Homocitrullylamino adenosine inhibits the incorporation of [ 14 C]amino acids into a hot acid-insoluble form in cell-free systems derived from Escherichia coli and rat liver. TheExpand
Formation of Dg-1-amino-2-propanol by a highly purified enzyme from Escherichia coli.
Effect of Cephalothin on Measurement of Creatinine Concentration
Clinicians should be aware of this phenomenon in patients receiving cephalothin, both when monitoring renal function and when assessing patient reliability in the collection of timed urine specimens. Expand
Seed Germination Studies. III. Properties of a Cell-free Amino Acid Incorporating System From Pea Cotyledons; Possible Origin of Cotyledonary α-Amylase
The possibility remains that the α-amylase is newly synthesized during germination, and the preparation and properties of a cell-free protein-synthesizing system from germinating pea cotyledons is described; polyuridylic acid must be added for l-phenylalanine incorporation. Expand
Purification, separation, and characterization of two molecular forms of D-1-amino-2-propanol:NAD+ oxidoreductase activity from extracts of Escherichia coli K-12.
Two molecular forms (designated Form L and Form S) of the oxidoreductase, both of which are catalytically active, have been separated by gel filtration on Sephadex G-200 and indicate that the two forms of the enzyme are different not only in size but also in shape. Expand
Urinary N-Acetyl-Glucosaminidase Excretion in Rats with Renovascular Hypertension 1
Preliminary observations in man have raised the possibility that the lysosomal acid hydrolase n-acetyl-glucosaminidase may be of value in identifying patients with renovascular hypertension, but in an accepted animal model of renov vascular hypertension, this suggestion is not supported. Expand