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|a eng
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| 100 |
1 |
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|a Brechtel, R
|e verfasserin
|4 aut
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| 245 |
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|a The lectin from the mushroom Pleurotus ostreatus
|b a phosphatase-activating protein that is closely associated with an alpha-galactosidase activity. A part of this paper has been presented as a preliminary report at the 17th Interlec. Meeting 1997 in Würzburg, Germany
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|c 2001
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Revised 30.09.2020
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|a published: Print
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|a Citation Status PubMed-not-MEDLINE
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|a The lectin from the mushroom Pleurotus ostreatus described earlier [F. Conrad, H. Rüdiger, The lectin from Pleurotus ostreatus: purification, characterization and interaction with a phosphatase, Phytochemistry 36 (1994) 277-283] was further characterized. Determination of the isoelectric point by capillary electrophoresis gave a value of 7.6. The dissociation constant of the lectin-alpha-lactose-1-phosphate complex determined by capillary electrophoresis is 3 mM. The activation of an endogenous phosphatase by the lectin as found earlier for the pseudosubstrate p-nitrophenylphosphate was confirmed also for naturally occurring substrates as ADP and ATP. We observed that at all purification steps the lectin is accompanied by an alpha-galactosidase activity. Both activities could neither be resolved by electrophoresis under non-denaturing conditions nor by affinity chromatography. However, carbohydrate binding by the lectin and carbohydrate processing by the enzyme are not due to the same site since: (i) the lectin accepts both alpha- and beta-glycosides whereas the enzyme activity is restricted to the alpha-anomer; (ii) the interaction with erythrocytes leads to a stable agglutinate, i.e. no 'clot-dissolving activity' [C.N. Hankins, J.I. Kindinger, L.M. Shannon, Legume alpha-galactosidases which have hemagglutinin properties, Plant Physiol. 65 (1980) 618-622] is observed; (iii) the alpha-galactosidase activity is inhibited by galactose but not by a beta-galactoside. Therefore, lectin and enzymatic activities are either properties of two tightly associated proteins, or of just one molecule. The kinetic parameters of the lectin-associated alpha-galactosidase activity for p-nitrophenyl-alpha-galactopyranoside are: K(M)=2.5 mM, k(cat)=66 s(-1), and K(I)=20mM for the inhibitor D-galactose
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| 650 |
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|a Journal Article
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| 700 |
1 |
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|a Wätzig, H
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Rüdiger, H
|e verfasserin
|4 aut
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| 773 |
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8 |
|i Enthalten in
|t Plant science : an international journal of experimental plant biology
|d 1985
|g 160(2001), 5 vom: 01. Apr., Seite 1025-1033
|w (DE-627)NLM098174193
|x 0168-9452
|7 nnns
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| 773 |
1 |
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|g volume:160
|g year:2001
|g number:5
|g day:01
|g month:04
|g pages:1025-1033
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