Isolation and characterization of a 30 kDa protein with antifungal activity from leaves of Engelmannia pinnatifida.
During the course of screening plants for novel antifungal activity, we found that a high-molecular-mass fraction of an extract from leaves of Engelmannia pinnatifida exhibited potent and broad-spectrum antifungal activity. In this study a 30 kDa protein from E. pinnatifida leaves was purified to homogeneity by ammonium sulphate precipitation, gel filtration, Mono-Q and C18 reverse-phase column chromatographies. The purified protein showed potent antifungal activity against various plant pathogens with as little as 50 ng. The N-terminal amino acid sequence of the purified protein was determined as XXTKFDFFTLALQXPAXF, where X indicates an unidentified residue. This sequence showed 35-50% sequence identity with purified style glycoproteins associated with self-incompatibility from wild tomato, tobacco and petunia, a phosphate-starvation-induced ribonuclease from cultured tomato cells and the SIR 63.4 kDa protein from yeast.
Huynh
Q K
QK
Department of Protein Biochemistry, Searle Research and Development, St. Louis, MO 63198, USA.
Borgmeyer
J R
JR
Smith
C E
CE
Bell
L D
LD
Shah
D M
DM
D000595:Amino Acid Sequence; D000935:Antifungal Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005658:Fungi / Q000187:drug effects*; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D018515:Plant Leaves; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D010944:Plants; D017386:Sequence Homology, Amino Acid
D000935:Antifungal Agents; D010940:Plant Proteins