Seed-specific aspartic proteinase FeAP12 from buckwheat (Fagopyrum esculentum Moench) | Zendy

Gordana Timotijević | Zendy; Mira Milisavljević | Zendy; Svetlana Radović | Zendy; Miroslav Konstantinović | Zendy; Vesna Maksimović | Zendy

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Seed-specific aspartic proteinase FeAP12 from buckwheat (Fagopyrum esculentum Moench)

Author(s) -

Gordana Timotijević,

Mira Milisavljević,

Svetlana Radović,

Miroslav Konstantinović,

Vesna Maksimović

Publication year - 2010

Publication title -

archives of biological sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.217

H-Index - 25

eISSN - 1821-4339

pISSN - 0354-4664

DOI - 10.2298/abs1001143t

Subject(s) - fagopyrum , biology , aspartic acid , botany , amino acid , complementary dna , gene , biochemistry

Aspartic proteinase gene (FeAP12) has been isolated from the cDNA library of developing buckwheat seeds. Analysis of its deduced amino acid sequence showed that it resembled the structure and shared high homology with typical plant aspartic proteinases (AP) characterized by the presence of a plant-specific insert (PSI), unique among APs. It was shown that FeAP12 mRNA was not present in the leaves, roots, steam and flowers, but was seed-specifically expressed. Moreover, the highest levels of FeAP12 expression were observed in the early stages of seed development, therefore suggesting its potential role in nucellar degradation

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