Purification and characterization of windmill palm tree (Trachycarpus fortunei) peroxidase.
High peroxidase activity was demonstrated to be present in the leaf of several species of cold-resistant palms. Histochemical studies of the leaf of windmill palm tree (Trachycarpus fortunei) showed the peroxidase activity to be localized in hypoderma, epidermis, cell walls, and conducting bundles. However, chlorophyll-containing mesophyll cells had no peroxidase at all. The leaf windmill palm tree peroxidase (WPTP) was purified to homogeneity and had a specific activity of 6230 units/mg, RZ = 3.0, a molecular mass of 50 kDa, and an isoelectric point of pI 3.5. The electronic spectrum of WPTP with a Soret band at 403 nm was typical of plant peroxidases. The N-terminal amino acid sequence of WPTP was determined. The substrate specificity of WPTP was distinct from that of other palm peroxidases, and the best substrate for WPTP was 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid). The palm peroxidase showed an unusually high stability at elevated temperatures and high concentrations of guanidine.
Caramyshev
Alexei V
AV
Department of Chemistry, M. V. Lomonosov Moscow State University, Moscow 119992, Russia.
Firsova
Yuliya N
YN
Slastya
Evgen A
EA
Tagaev
Andrei A
AA
Potapenko
Nataly V
NV
Lobakova
Elena S
ES
Pletjushkina
Olga Yu
OY
Sakharov
Ivan Yu
IY
D000595:Amino Acid Sequence; D028023:Arecaceae / Q000201:enzymology*; D002118:Calcium / Q000032:analysis; D004795:Enzyme Stability; D006861:Hydrogen Peroxide / Q000378:metabolism; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009195:Peroxidase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D018515:Plant Leaves / Q000201:enzymology; D013379:Substrate Specificity
D006861:Hydrogen Peroxide; D009195:Peroxidase; D002118:Calcium