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1
Content available remote

Purification and properties of lectin from potato tubers and leaves; Interaction with acid phosphatase from potato tuber

100%
Wierzba-Arabska E., Morawiecka B.
|
|
issue 4
407-420
2
Content available remote

Acid phosphatase of potato tubers (Solanum tuberosum L). Purification, properties, sugar and amino acid composition

100%
Kruzel M., Morawiecka B.
Acta Biochimica Polonica
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1982
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vol. 29
|
issue 3-4
321-330
3
Content available remote

Purification and some properties of the main polymorphic form of acid phosphatase from Poa pratensis seeds

100%
Lorenc-Kubis I., Morawiecka B.
Acta Biochimica Polonica
|
1980
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vol. 27
|
issue 3-4
345-352
4
Content available remote

The N-acetylgalactosamine and lactosamine specific lectin from Iris hybrida leaves

81%
Ferens-Sieczkowska M., Orczyk-Pawiłowicz M., Morawiecka B.
Acta Biochimica Polonica
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1997
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vol. 44
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issue 2
301-307
5
Content available remote

Plant purple acid phosphatases - genes, structures and biological function.

81%
Olczak M., Morawiecka B., Wątorek W.
|
2003
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vol. 50
|
issue 4
1245-1256
EN
The properties of plant purple acid phosphatases (PAPs), metallophosphoesterases present in some bacteria, plants and animals are reviewed. All members of this group contain a characteristic set of seven amino-acid residues involved in metal ligation. Animal PAPs contain a binuclear metallic center composed of two irons, whereas in plant PAPs one iron ion is joined by zinc or manganese ion. Among plant PAPs two groups can be distinguished: small PAPs, monomeric proteins with molecular mass around 35 kDa, structurally close to mammalian PAPs, and large PAPs, homodimeric proteins with a single polypeptide of about 55 kDa. Large plant PAPs exhibit two types of structural organization. One type comprises enzymes with subunits bound by a disulfide bridge formed by cysteines located in the C-terminal region around position 350. In the second type no cysteines are located in this position and no disulfide bridges are formed between subunits. Differences in structural organisation are reflected in substrate preferences. Recent data reveal in plants the occurrence of metallophosphoesterases structurally different from small or large PAPs but with metal-ligating sequences characteristic for PAPs and expressing pronounced specificity towards phytate or diphosphate nucleosides and inorganic pyrophosphate.
6
Content available remote

Developmental differences in acid phosphatase and agglutination activity in roots of Cucurbita ficifolia seedlings. Purification and some properties of lectin

81%
Lorene-Kubis I., Krawców A., Morawiecka B.
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7
Content available remote

Acid phosphatase of the yeast Rhodotorula rubra. Purification and properties of the enzyme

80%
Wątorek W., Morawiecka B., Korczak B.
Acta Biochimica Polonica
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1977
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vol. 24
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issue 2
153-162
8
Content available remote

GalNAc/Gal specific lectin from German iris (Iris germanica L.) rootstock

80%
Ferens-Sieczkowska M., Morawiecka B.
|
|
vol. 40
|
issue 1
123-124
9
Content available remote

Lectisis from squash (Cucurbita ficifolia) seedlings

70%
Lorenc-Kubis I., Klimczak A., Morawiecka B.
|
10
Content available remote

Function of carbohydrate moiety in acid phosphatase of Rhodotorula glutinis

70%
Wątorek W., Morawiecka B.
Acta Biochimica Polonica
|
1984
|
vol. 31
|
issue 2
217-221
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