Quality Standard of Qiang Herb Sophora davidii var.chuansiensis

[Objectives]To establish the quality standard of common clinical folk herb Sophora davidii var.chuansiensis.[Methods]The qualitative identification was performed by microscopic method and thin-layer chromatography(TLC).The contents of moisture,total ash,acid insoluble ash and extract were determined according to the methods of the Chinese Pharmacopoeia(2020).High performance liquid chromatography(HPLC)was used to determine the contents of oxymatrine and oxysophocarpine.[Results]The microscopic characteristics were obvious,including crystal sheath fiber,calcium oxalate square crystal,non glandular hair,stone cells,epidermal cells,stomata,cork cells,vessels with marginal pits and so on.TLC spots were clear,and the resolution was good.The contents of moisture,total ash,acid insoluble ash and extract from 10 batches of samples were 4.70%-8.33%,3.43%-4.19%,0.65%-1.02%and 14.67%-22.04%respectively.The determination results of oxymatrine were between 0.10%-0.33%,with an average value of 0.19%.The determination results of sophocarpine oxide were between 0.30%-0.38%,with an average value of 0.34%.[Conclusions]The established quality standard of S.davidii var.chuansiensis had good specificity and accuracy,and could be used for the quality control of herb S.davidii var.chuansiensis.

Characterization and Expression of Outer Membrane Protein A I Gene of Aeromonas veronii

The outer membrane protein, ompA, ofAeromonas veronii has a role in the virulence of the organism and is a potential candidate for vaccine development. In this study, ompA I ofAeromonas veronii strain WA106 was cloned and sequenced, then, it was expressed in Escherichia coli BL21. The nucleotide sequence of ompA I gene was 1 023 base pairs （GenBank Accession NO.KC748024）, which showed 100% homology with that of A. veronii （NO.AB290200.1）. This predicted protein was composed of 340 amino acid residues. Its molecular weight was 35.78 ku and isoelectric point was 5.18. The protein was a hydrophilic protein containing alpha helix and random coil with percentage of 35.0% and 49.7%, respectively. The tertiary structure, quaternary structure prediction showed that ompA I protein contained two peptide chains. SDS-PAGE showed that the actual value of the fusion protein was consistent with the expected result. It will facilitate further study of the role of ompA I protein.

Identification of human LDHC4 as a potential target for anticancer drug discovery

One of the distinct hallmarks of cancer cells is aerobic glycolysis(Warburg effect). Lactate dehydrogenase A(LDHA) is thought to play a key role in aerobic glycolysis and has been extensively studied, while lactate dehydrogenase C(LDHC), an isoform of LDHA, has received much less attention.Here we showed that human LDHC was significantly expressed in lung cancer tissues, overexpression of Ldhc in mice could promote tumor growth, and knock-down of LDHC could inhibit the proliferation of lung cancer A549 cells. We solved the first crystal structure of human LDHC4 and found that the activesite loop of LDHC4 adopted a distinct conformation compared to LDHA4 and lactate dehydrogenase B4(LDHB4). Moreover, we found that(ethylamino)(oxo)acetic acid shows about 10 times selective inhibition against LDHC4 over LDHA4 and LDHB4. Our studies suggest that LDHC4 is a potential target for anticancer drug discovery and(ethylamino)(oxo)acetic acid provides a good start to develop lead compounds for selective drugs targeting LDHC4.