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1

Profiles of quinolizidine alkaloids and their ester conjugates in white lupin (Lupinus albus L.) plants treated with fungal elicitors or abiotic factors

100%
Stobiecki M., Wojtaszek P., Pislewska M.
Biological Bulletin of Poznań. Supplement
|
1995
|
tom 32
2

Lupin phytoalexins - reality or fantasy?

100%
Wojtaszek P., Stobiecki M., Pislewska M.
Biological Bulletin of Poznań. Supplement
|
1995
|
tom 32
3

Exocellular pathogenesis defence-related [glyco]proteins from suspension-cultured Lupinus albus cells

100%
Wojtaszek P., Pislewska M., Bolwell G. P., Stobiecki M.
Biological Bulletin of Poznań. Supplement
|
1997
|
tom 34
4

Secretion of stress-related proteins by suspension-cultured Lupinus albus cells

100%
Wojtaszek P., Pislewska M., Bolwell G. P., Stobiecki M.
Acta Biochimica Polonica
|
1998
|
tom 45
|
nr 1
A suspension culture of white lupin cells has been established, and proteins of the exocellular matrix analysed. Based on homologies of N-terminal amino-acid sequences, three stress- or defence-related proteins: acidic class III chitinase, polygalacturonase-inhibiting protein, and germinóxalate oxidase, secreted by lupin cell culture, were identified.
5

Active chitinases in the apoplastic fluids of healthy white lupin [Lupinus albus L.] plants

100%
Burzynski A., Pislewska M., Wojtaszek P.
Acta Physiologiae Plantarum
|
2000
|
tom 22
|
nr 1
6

Secondary metabolites in elicitor-treated Lupinus albus plants and suspension-cultured cells

100%
Bednarek P., Stobiecki M., Pislewska M., Wojtaszek P.
Biological Bulletin of Poznań. Supplement
|
1997
|
tom 34
7

Exocellular [glyco]proteins of Lupinus albus plants and suspension-cultured cells

100%
Wojtaszek P., Pislewska M., Bolwell G. P.
Acta Physiologiae Plantarum
|
1998
|
tom 20
|
nr 3
Plant species from genus Lupinus are among the oldest known legumes, and various aspects of their biology are considerably different from those commonly observed within Leguminosae. To study this issue in more detail, a suspension culture of Lupinus albus cells was developed, and the glycosylation patterns of exocellular proteins analysed. N-linked oligosaccharide side-chains were detected with two lectins: concanavalin A (ConA) and wheat germ agglutinin (WGA) used with respective anti-lectin antibodies, while O-linked arabinosylated side-chains of (hydroxy)proline-rich glycoproteins were identified with anti-(42 kDa French bean chitin-binding protein) antibodies. The obtained data were compared with analogous ones for exocellular (glyco)proteins from suspension-cultured Phaseolus vulgaris cells and from various tissues of L. albus plants. Major species-specific differences between exocellular (glyco)proteins from lupin and bean cells were identified. Similarly, developmentally regulated glycosylation changes following transition from organised plant tissue to dedifferentiated suspension-cultured lupin cells were detected and analysed.
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