Aim To investigate the effect of SM-1 on seven main cytochrome P450(CYP450)in human liver microsomes.Methods Substrate or SM-1 was incubated with human liver microsomes for 30 min in vitro,and divided into control group and experimental group.The effects of SM-1 on the main phase I metabolic enzymes in human liver microsomes was detected by HPLC.Phenacetin,bupropion,paclitaxel,tolbutamide,omeprazole,dextromethorphan,testosterone were investigated as probe drugs.Results Inhibition rate of SM-1 on the classical substrate of human liver microsomal CYP was 0.05％,3.37％,0.08％,2.07％,4.20％,-0.15％and 10.84％,respectively.Conclusions SM-1 may have inhibitory effect on CYP3A4.Attention should be paid to the interaction of clinical drug induced by CYP enzyme inhibition.

Protein tyrosine phosphatase 1B(PTP1B),a member of protein tyrosine phosphatases(PTPs),plays a key role in the negative regulation of insulin and leptin signalings.Recent studies showed that PTP1B had an important connection with endoplasmic reticulum(ER)stress, pancreatic beta cells proliferation and insulin secretion,and is closely related to the pathological process of type 2 diabetes mellitus(T2DM)and obesity. Therefore,PIP1B targeted inhibitors have become a research hotspot in the treatment of these metabolic disea-ses.Based on the structural features of PTP1B and its relationship with T2DM and obesity,PTP1B inhibitors were classified according to the sites of binding.Their latest research advances were reviewed in this paper,providing a reference for the development of anti-T2DM and anti-obesity drugs targeting PTP1B.

In order to clone and express alcohol dehydrogenase II (ADH2) gene from Saccharomyces cerevisiae in E. coli BL21 (DE3) efficiently, we extracted the total RNA as template and obtained ADH2 gene by RT-PCR and connected ADH2 gene to pTAT plasmids to gain recombinant expression plasmid pTAT-ADH2, then transformed this recombinant expression plasmid pTAT-ADH2 into E. coli BL21 (DE3). The recombinant was induced by IPTG to express ADH2. After purification, ADH2 activity was tested in vitro and toxicologic test was done in mouse. Sequence test showed that the acquired fragments exhibited 90% homology to ADH2 gene sequence from GenBank report. The target gene expressed efficiently and took up to approximant 50% of total protein by SDS-PAGE and band scanning analysis. The purified protein exhibited the identified activity through biochemical test and mouse toxicological test. As a result, the acquired ADH2 gene was highly homology to the published sequence and expressed at a high level in E. coli BL21 (DE3), more importantly, ADH2 proved to have ethanol dehydrogenase activity.
Alcohol Dehydrogenase ; genetics ; isolation & purification ; Animals ; Cloning, Molecular ; Escherichia coli ; genetics ; metabolism ; Genetic Vectors ; Mice ; Random Allocation ; Recombinant Proteins ; biosynthesis ; genetics ; isolation & purification ; Saccharomyces cerevisiae ; enzymology ; genetics ; Saccharomyces cerevisiae Proteins ; genetics ; isolation & purification