Prolyl iminopeptidase from seeds of sunflower (Helianthus annuus L.)

• Autorzy: Tishinov K. , Petrova S. , Nedkov P.
• Języki publikacji: EN

Abstrakty

EN

Prolyl iminopeptidase from sunflower seed (Helianthus annuus L.) was purified to molecular homogeneity. It is a 105-kDa heterodimer consisting of two subunits: 53 and 55 kDa. It has pI of 6.2 and optimal activity at pH 8.0–8.5 and 45–50℃. The inhibitory analysis was inconclusive about its catalytic machinery, as a significant degree of modification was not observed with any of the used diagnostic inhibitors. Its specificity is restricted to removal of N-terminal prolyl residues.

• Wydawca: -
• Czasopismo: Acta Physiologiae Plantarum
• Rocznik: 2010
• Tom: 32
• Numer: 1
• Opis fizyczny: p.211-213,fig.,ref.

Twórcy

autor

Tishinov K.

• Franciszek Górski Institute of Plant Physiology of the Polish Academy of Sciences

autor

Petrova S.

• Franciszek Górski Institute of Plant Physiology of the Polish Academy of Sciences

autor

Nedkov P.

• Franciszek Górski Institute of Plant Physiology of the Polish Academy of Sciences

Bibliografia

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