Two isoforms of a nucleotide‐sugar pyrophosphatase/phosphodiesterase from barley leaves (Hordeum vulgare L.) are distinct oligomers of HvGLP1, a germin‐like protein

FEBS Letters

Akazawa, Takashi¹  Baroja-Fernández, Edurne¹  Pozueta-Romero, Javier¹  Zandueta-Criado, Aitor¹  Muñoz, Francisco José¹  Rodrı́guez-López, Milagros¹  Moreno-Bruna, Beatriz¹ 

[1] Instituto de Agrobiotecnologı́a y Recursos Naturales, Universidad Pública de Navarra/Consejo Superior de Investigaciones Cientı́ficas, Ctra. Mutilva s/n, 31192 Mutilva Baja, Navarra, Spain

关键词: Cell wall;    Cupin;    Gluconeogenesis;    ADPG;    ADPglucose;    AGPPase;    ADPG pyrophosphatase/phosphodiesterase;    GLP;    germin-like protein;    HvGLP1;    Hordeum vulgare germin-like protein 1;    PAGE;    polyacrylamide gel electrophoresis;    PNPP;    p-nitrophenyl phosphate;    SAGPPase;    soluble ADPglucose pyrophosphatase/phosphodiesterase;    UDPG;    UDPglucose;   

DOI  :  10.1016/S0014-5793(01)02135-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two isoforms of ADPglucose pyrophosphatase/phosphodiesterase (AGPPase) have been characterized using barley leaves (Hordeum vulgare L.). Whilst one of the isoforms, designated as soluble AGPPase1 (SAGPPase1), is soluble in low ionic strength buffers, the other, SAGPPase2, is extractable using cell wall hydrolytic enzymes or high salt concentration solutions, thus indicating that it is adventitiously bound to the cell wall. Both AGPPase isoforms are highly resistant to SDS, this characteristic being utilized to purify them to homogeneity after zymographic detection of AGPPase activity in SDS-containing gels. N-terminal and internal amino acid sequencing analyses revealed that both SAGPPase1 and SAGPPase2 are distinct oligomers of the previously designated HvGLP1, which is a member of the ubiquitously distributed group of proteins of unknown function designated as germin-like proteins (GLPs).

【 授权许可】

Unknown