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1.
Amino Acids ; 4(3): 303-6, 1993 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-24190610

RESUMO

3-Fluorotyrosine fluorescence is quenched effectively by phosphate ions not only by a dynamic but also by a static mechanism owing to H-bond complex formation in ground state. 3-Fluorotyrosine pKa values both in the ground and first excited state (8.3 and 4, respectively) are appreciably lower than those of tyrosine, thus promoting 3-fluorotyrosinate ion formation in the excited state. Additional emission owing to 3-fluorotyrosinate ion (near 350 nm) may be taken erroneously for tryptophan fluorescence.

2.
Amino Acids ; 5(1): 99-101, 1993 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-24190648

RESUMO

Racemic N-Boc-4-difluoromethoxyphenylglycine was prepared by O-difluoromethylation of D-N-Boc-4-hydroxyphenylglycine under basic conditions, whereas the hexafluoropropylation reaction gives optically pure D-N-Boc-4-hexafluoropropoxyphenylglycine. D,L-4-difluoromethoxyphenylglycine was obtained by the action of TFA on the corresponding amino acid derivative.

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