Daniel S. Hodgins
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View article: Phenylalanine ammonia-lyase. Induction and purification from yeast and clearance in mammals.
Phenylalanine ammonia-lyase. Induction and purification from yeast and clearance in mammals. Open
Yeast phenylalanine ammonia-lyase (EC 4.3.1.5) catalyzes the deamination of L-phenylalanine to form trans-cinnamic acid and tyrosine to trans-coumaric acid. Maximal enzyme activity in Rhodotorula glutinis (2 units/g, wet weight, of yeast) …
View article: Adenylate Cyclase in Islets of Langerhans
Adenylate Cyclase in Islets of Langerhans Open
An improved method for the isolation of rat pancreatic islets possessing adenylate cyclase responsive to various hormones and agents is described.
View article: Yeast Phenylalanine Ammonia-lyase
Yeast Phenylalanine Ammonia-lyase Open
Phenylalanine ammonia-lyase from the yeast Rhodotorula glutinis was purified by salt fractionations and Sephadex chromatography. Density gradient centrifugation and Sephadex chromatography indicated its molecular weight to be about 275,000…
View article: The Presence of Covalently Bound Pyruvate in d-Proline Reductase and Its Participation in the Catalytic Process
The Presence of Covalently Bound Pyruvate in d-Proline Reductase and Its Participation in the Catalytic Process Open
d-Proline reductase contains covalently bound pyruvate, which is probably bonded to the protein through an amide linkage. Reduction of the pyruvate carbonyl group leads to loss of enzyme activity. It is postulated that the nitrogen atom of…