| Autor: |
Allen AK; Department of Biochemistry, Charing Cross and Westminster Medical School, (University of London), U.K., Bolwell GP, Brown DS, Sidebottom C, Slabas AR |
| Jazyk: |
angličtina |
| Zdroj: |
The international journal of biochemistry & cell biology [Int J Biochem Cell Biol] 1996 Nov; Vol. 28 (11), pp. 1285-91. |
| DOI: |
10.1016/s1357-2725(96)00043-x |
| Abstrakt: |
Potato (Solanum tuberosum) tuber lectin is a chitin-binding, hydroxyproline-rich glycoprotein, which may be involved in the defence mechanism of the plant. We had previously obtained evidence that it consists of at least two very dissimilar domains. The aim was to use a combination of accurate determinations of molecular weight and protein sequencing to gain more accurate information on the domains. Accurate determinations of the molecular weight of the lectin by a MALDI mass spectrometer have shown that the subunit molecular weight is 65,500 (+/- 1100) and that of a totally deglycosylated sample is 31,250 (+/- 30). This means that the lectin is 52.3 (+/- 1)% carbohydrate with a considerable number of glycoforms being present. Partial sequences and other analyses are consistent with the existence of three distinct domains. These are: (1) an N-terminal region which is rich in proline but poor in hydroxyproline; (2) a glycosylated region with a glycosylated molecular weight of 45,300 (+/- 1100) and a deglycosylated molecular weight of 11,050 (+/- 50) which is extremely rich in glycosylated hydroxyproline residues with a similar sequence to extensins; and (3) a cystine-rich domain which has the sugar binding site shows partial conservation of a repeated motif common to many chitin-binding proteins of the hevin family including wheat-germ agglutinin. The closest similarity seems to be to the sequence of potato basic chitinase. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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