FURTHER STUDIES ON THE DUAL REQUIREMENT FOR PHENYLALANINE AND TYROSINE IN TISSUE CULTURE

1961 ◽  
Vol 39 (5) ◽  
pp. 925-932 ◽  
Author(s):  
Helen J. Morton ◽  
Joseph F. Morgan

Seventeen structurally related compounds were tested for their ability to substitute for phenylalanine or tyrosine in the nutrition of chick embryo heart fragments. DL-Alanyl-DL-phenylalanine replaced phenylalanine. All other compounds had negligible effects, and most were toxic at high concentrations. β-Phenylserine, a phenylalanine antagonist, actually prolonged the survival of chick heart cells but only if both phenylalanine and tyrosine were present. Similarly, optimal reversal of β-phenylserine toxicity was dependent on the presence of both amino acids. Although phenylalanine and tyrosine are not interconvertible in the present system, it has been shown that three phenylalanine antagonists, p-fluorophenylalanine, β-2-thienylalanine, and β-phenylserine, can be identified by their relationship to tyrosine, rather than to phenylalanine.

1971 ◽  
Vol 122 (4) ◽  
pp. 409-414 ◽  
Author(s):  
G. G. Guidotti ◽  
A. F. Borghetti ◽  
Britta Lüneburg ◽  
G. C. Gazzola

1. Isolated chick embryo heart cells were used to investigate the mode of action of insulin on the transport of three naturally occurring amino acids: l-proline, l-serine and glycine. Initial velocities of uptake were measured over a period of 5min with an 80-fold range of amino acid concentration. Corrections for amino acid diffusion, incorporation into protein and conversion into carbon dioxide were introduced. 2. The uptake processes approximated Michaelis–Menten kinetics within definite ranges of amino acid concentrations. A single transport system for proline and at least two transport systems for serine and glycine were detected. 3. The kinetic effects of insulin on transport systems for the amino acids tested were consistent with an acceleration of the maximal velocity of the process, without substantial changes in substrate concentration for half-maximal transport velocity. 4. These hormonal effects were not essentially altered by the corrections for amino acid incorporation into protein and conversion into carbon dioxide.


1984 ◽  
Vol 152 (2) ◽  
pp. 427-435 ◽  
Author(s):  
Gunilla Norrgren ◽  
Ted Ebendal ◽  
Herman Wikström

1980 ◽  
Vol 20 (1) ◽  
pp. 45-57 ◽  
Author(s):  
Y. Dickstein ◽  
H. Schwartz ◽  
J. Gross ◽  
A. Gordon

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