[Percutaneous vertebroplasty for the treatment of acute burst thoracolumbar fractures].

OBJECTIVE: To explore the feasibility of percutaneous vertebroplasty for the treatment of acute burst thoracolumbar fracture. METHODS: Fifty-eight patients (male 38 and female 20, ranging in age from 38 to 70 years, with an average of 56.8 years) with acute burst thoracolumbar fracture were treated by percutaneous vertebroplasty. The injuried vertebrae were T11 in 3 cases, T12 18 cases, L1 29 cases, L2 5 cases and L3 3 cases. All suited cases were classified into 3 types according to injuried vertebral shapes,type I (safe type 26 cases), type II (risk type 21 cases), and type III (marginal type 11 cases). RESULTS: All the patients were followed up ranging from 1 to 2.5 years (mean 1.6 years). Fifty-three patients could walk in 1 to 3 days after operation. Among 55 patients who obtained complete recovery (CR), 39 patients could do daily works and 16 patients could do houseworks. The CR rate was 95%. Three patients who obtained partial recovery (PR), could live by themselves and felt slight lumbago after movements. The PR rate was 5%. CONCLUSION: Percutaneous vertebroplasty for the treatment of acute burst thoracolumbar fracture is a feasible and effective method even for particular risks.

[Purification and characterization of a novel alpha-galactosidase from penicillium sp. F63 CGMCC1669].

An a-galactosidase-producing fungus was screened out of 26 filamentous fungi isolated from soil by us. Phylogenetic analysis based on the alignment of 18S rDNA sequences, combined with the morphological identification, indicated that the strain F63 was a member of the genus Penicillium. The a-galactosidase from Penicillium sp. F63 was purified to apparent homogeneity by ammonium sulfate precipitation, ion-exchange and gel filtration chromatography. The molecular size of the purified enzyme is approximately 82kDa estimated by SDS-PAGE. The a-galactosidase has an optimum pH of 5.0 and an optimum temperature of 45 degrees C. The enzyme is stable between pH5.0 and 6.0 below 40 degrees C. The a-galactosidase activity is slightly inhibited by Ag+ , which is dissimilar to other a-galactosidases. Kinetic studies of the a-galactosidase showed that the Km and the Vmax for pNPG are 1.4mmol/L and 1.556mmol/L. min(-1) x mg- 1, respectively. The enzyme is able to degrade natural substrates such as melibiose, raffinose and stachyose but not galactose-containing polysaccharides. The alpha-galactosidase was identified by MALDI-TOF-MS and its inner peptides were sequenced by ESI-MS/MS. The results show that the a-galactosidase is a novel one.