Characterization of an aspartic proteinase activity in buckwheat (Fagopyrum esculentum Moench) seeds.
The pepstatin A sensitive acidic proteolytic activity of total protein extracts of buckwheat seeds has been analyzed in developing, mature, and germinating seeds by activity measurements as well as by electrophoretic and immunochemical techniques. Immunoblot analysis using cross-reactive antibodies raised against barley phytepsin suggested that specific proteolytic activity could be attributed to a 47 kDa heterodimeric polypeptide, composed of two subunits: 31 and 16 kDa polypeptides. The analysis of time course expression revealed that the 47 kDa heterodimer accumulated during seed maturation starting from 12 days after pollination and was also present at the beginning of germination. Milk-clotting activity of this proteinase was also indicated.
Timotijevic
Gordana S
GS
Institute of Molecular Genetics and Genetic Engineering, Belgrade, Yugoslavia.
Radovic
Svetlana R
SR
Maksimovic
Vesna R
VR
D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D002364:Caseins / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D019612:Fagopyrum / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008892:Milk / Q000737:chemistry; D010936:Plant Extracts / Q000737:chemistry; D012639:Seeds / Q000201:enzymology*
D002364:Caseins; D010936:Plant Extracts; D016282:Aspartic Acid Endopeptidases