Glycine‐enhanced inhibition of rat liver nucleotide pyrophosphatase/phosphodiesterase‐I by EDTA: a full account of the reported inhibition by commercial preparations of acidic fibroblast growth factor (FGF‐1)

FEBS Letters

Romero, Ana²  Ávalos, Martı́n¹  Cameselle, José Carlos²  López-Gómez, Juan²  Meireles Ribeiro, João²  Costas, Marı́a Jesús²  Fernández, Ascensión² 

[1] Departamento de Quı́mica Orgánica, Facultad de Ciencias, Universidad de Extremadura, E-06071 Badajoz, Spain;Unidad de Bioquı́mica y Biologı́a Molecular, Facultad de Medicina, Universidad de Extremadura, Apartado 108, E-06080 Badajoz, Spain

关键词: Nucleotide pyrophosphatase;    Phosphodiesterase I;    Fibroblast growth factor;    acidic;    Glycine;    EDTA;    Rat liver;    FGF-1;    acidic fibroblast growth factor;    NPP/PDE;    nucleotide pyrophosphatase/phosphodiesterase I;   

DOI  :  10.1016/S0014-5793(97)01536-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The earlier reported inhibition of rat liver nucleotide pyrophosphatase/phosphodiesterase I (EC 3.1.6.9/EC 3.1.4.1; NPP/PDE) by culture-grade acidic fibroblast growth factor (FGF-1) correlates with a low-M _r contaminant. ¹H-NMR analyses revealed EDTA in the total-volume fractions of a gel-filtration experiment, where all the inhibitory activity of the FGF-1 preparation was recovered. NPP/PDE inhibition by EDTA (and by unfractionated FGF-1 or the EDTA-containing fractions) was time-dependent, blocked by the substrate p-nitrophenyl-dTMP, and strongly enhanced by glycine. The use of glycine buffers in earlier work was critical to the apparent inhibition by FGF-1. The results point to a conformational change favored by glycine that may be relevant to the biological role of NPP/PDE.

【 授权许可】

Unknown