Purification and characterization of an antifungal thaumatin-like protein from Cassia didymobotrya cell culture

A 23-kDa antifungal thaumatin-like protein was isolated and purified from Cassia didymobotrya (Fres.) cell cultures for the first time. The protein was secreted in the culture medium, but it could be also isolated after elution of whole cells with a 0.5 M CaCl(2) solution. Treatment of the cells wit...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 44(2006), 10 vom: 01. Okt., Seite 604-10
1. Verfasser: Vitali, A (VerfasserIn)
Weitere Verfasser: Pacini, L, Bordi, E, De Mori, P, Pucillo, L, Maras, B, Botta, B, Brancaccio, A, Giardina, B
Format: Aufsatz
Sprache:English
Veröffentlicht: 2006
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Antifungal Agents Plant Proteins
LEADER 01000naa a22002652 4500
001 NLM166129801
003 DE-627
005 20231223110147.0
007 tu
008 231223s2006 xx ||||| 00| ||eng c
028 5 2 |a pubmed24n0554.xml 
035 |a (DE-627)NLM166129801 
035 |a (NLM)17056265 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Vitali, A  |e verfasserin  |4 aut 
245 1 0 |a Purification and characterization of an antifungal thaumatin-like protein from Cassia didymobotrya cell culture 
264 1 |c 2006 
336 |a Text  |b txt  |2 rdacontent 
337 |a ohne Hilfsmittel zu benutzen  |b n  |2 rdamedia 
338 |a Band  |b nc  |2 rdacarrier 
500 |a Date Completed 01.02.2007 
500 |a Date Revised 30.09.2020 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a A 23-kDa antifungal thaumatin-like protein was isolated and purified from Cassia didymobotrya (Fres.) cell cultures for the first time. The protein was secreted in the culture medium, but it could be also isolated after elution of whole cells with a 0.5 M CaCl(2) solution. Treatment of the cells with laminarin oligosaccharides or salicylic acid, but not with NaCl, resulted in enhancement of expression of the protein. A rapid purification protocol was used based on cationic exchange chromatography. The protein, with a highly basic character (pI 10), has an exact molecular mass of 23034 Da, as determined by MALDI-ToF mass spectrometry analysis. N-terminal sequencing of the intact polypeptide and the sequencing of two internal tryptic peptides indicated significant identity with other thaumatin-like proteins (TLP). The protein exerted antifungal activity towards some Candida species showing EC(50) values comparable to those of other antifungal TLPs. The collected data lead to classify this TLP as a new PR-5 protein 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Antifungal Agents  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
700 1 |a Pacini, L  |e verfasserin  |4 aut 
700 1 |a Bordi, E  |e verfasserin  |4 aut 
700 1 |a De Mori, P  |e verfasserin  |4 aut 
700 1 |a Pucillo, L  |e verfasserin  |4 aut 
700 1 |a Maras, B  |e verfasserin  |4 aut 
700 1 |a Botta, B  |e verfasserin  |4 aut 
700 1 |a Brancaccio, A  |e verfasserin  |4 aut 
700 1 |a Giardina, B  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Plant physiology and biochemistry : PPB  |d 1991  |g 44(2006), 10 vom: 01. Okt., Seite 604-10  |w (DE-627)NLM098178261  |x 1873-2690  |7 nnns 
773 1 8 |g volume:44  |g year:2006  |g number:10  |g day:01  |g month:10  |g pages:604-10 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_350 
951 |a AR 
952 |d 44  |j 2006  |e 10  |b 01  |c 10  |h 604-10