Active aspartic proteinase is isolated from Brassica napus seeds and the peptide sequence is used to generate primers for PCR. We present here cDNA and genomic clones for aspartic proteinases from the closely related Brassicaceae Arabidopsis thaliana and Brassica napus. The Arabidopsis cDNA represents a single gene, while Brassica has at least 4 genes. Like other plant aspartic proteases, the two Brassicaceae enzymes contain an extra protein domain of about 100 amino acids relative to the mammalian forms. The intron/exon arrangement in the Brassica genomic clone is significantly different from that in mammalian genes. As the proteinase is isolated from seeds, the same tissue where 2S albumins are processed, this implies expression of one of...
Oligonucleotide primers based on conserved regions of the aspergillopepsins (EC 3.4.23.18) were used...
Unique to aspartic proteinases from plants are the presence of approximately 100 amino acid regions,...
An aspartic proteinase PEP2 [EC 3.4.23.25] was purified from a cell wall fraction of Aspergillus fum...
Active aspartic proteinase is isolated from Brassica napus seeds and the peptide sequence is used to...
A novel type of aspartic proteinase gene was isolated from the cDNA library of developing buckwheat ...
Two types of aspartic proteinase (AP) genes have been isolated from the cDNA library of developing b...
Aspartic proteases (APs), a large family of proteolytic enzymes with diverse functions, play importa...
Botrytis cinerea, an important fungal plant pathogen, secretes aspartic proteinase (AP) activity in ...
The most abundant isoform of the 2S albumin present in seeds of Arabidopsis thaliana has been sequen...
Aspartic proteases are proteolytic enzymes widely distributed in living organisms and viruses. Altho...
The ascomycete plant pathogen Botrytis cinerea secretes aspartic proteinase (AP) activity. Functiona...
A clone encoding a plastid isoenzyme of aspartate amino-transferase (AAT5) was isolated from an Arab...
Background - Phytophthora species are oomycete plant pathogens with such major social and economic i...
Typical aspartic proteinases from plants of the Astereaceae family like cardosins and cyprosins are ...
A cDNA clone, NA-PI-II, encoding a protein with partia1 identity to proteinase inhibitor (Pl) II of ...
Oligonucleotide primers based on conserved regions of the aspergillopepsins (EC 3.4.23.18) were used...
Unique to aspartic proteinases from plants are the presence of approximately 100 amino acid regions,...
An aspartic proteinase PEP2 [EC 3.4.23.25] was purified from a cell wall fraction of Aspergillus fum...
Active aspartic proteinase is isolated from Brassica napus seeds and the peptide sequence is used to...
A novel type of aspartic proteinase gene was isolated from the cDNA library of developing buckwheat ...
Two types of aspartic proteinase (AP) genes have been isolated from the cDNA library of developing b...
Aspartic proteases (APs), a large family of proteolytic enzymes with diverse functions, play importa...
Botrytis cinerea, an important fungal plant pathogen, secretes aspartic proteinase (AP) activity in ...
The most abundant isoform of the 2S albumin present in seeds of Arabidopsis thaliana has been sequen...
Aspartic proteases are proteolytic enzymes widely distributed in living organisms and viruses. Altho...
The ascomycete plant pathogen Botrytis cinerea secretes aspartic proteinase (AP) activity. Functiona...
A clone encoding a plastid isoenzyme of aspartate amino-transferase (AAT5) was isolated from an Arab...
Background - Phytophthora species are oomycete plant pathogens with such major social and economic i...
Typical aspartic proteinases from plants of the Astereaceae family like cardosins and cyprosins are ...
A cDNA clone, NA-PI-II, encoding a protein with partia1 identity to proteinase inhibitor (Pl) II of ...
Oligonucleotide primers based on conserved regions of the aspergillopepsins (EC 3.4.23.18) were used...
Unique to aspartic proteinases from plants are the presence of approximately 100 amino acid regions,...
An aspartic proteinase PEP2 [EC 3.4.23.25] was purified from a cell wall fraction of Aspergillus fum...