Objective To investigate the relationship between metabolism syndrome (MS) and fatty liver. Methods Plasma lipids, plasma glucose, liver function, blood pressure, body height and body weight were determined in 666 leaders receiving physical examination. Their livers were also examined by ultrasound. Whit analysis of variance and chi-square test, the effect of plasma lipids, plasma glucose, blood pressure, and weight index on fatty liver, and the relation between MS and fatty liver were analyzed. Results The weight index, systolic pressure, diastolic pressure, and the levels of total cholesterol, triglyceride, apolipoprotein B and plasma glucose in the patients with fatty liver were higher than those in healthy subjects. The levels of high-density lipoprotein and apolipoprotein A were lower in patients with fatty liver than those in healthy subjects. The morbidity of fatty liver in the patients with MS was higher than that in healthy subjects. Conclusion There was a close relation between MS and fatty liver. It was necessary to early treat MS.

Objective To investigate hemodynamie change in uremia complicating heart failure of elderly patients. Methods Totally 241 cases with uremia complicating heart failure received measurement of circulation dynamic detection(CD).The volume load,myocardial contractility and blood pressure were analyzed in the elderly group aged(71±6)years (n=116) and young and middleaged group aged(38± 10)years(n =125). Results The central venous pressure(CVP)[(26.7±11.3)cmH2O vs.(23.6 ± 10.7) cm H2O,t=2.410,P =0.010],effective circulation volume (ECV)[(4362± 1340)ml vs.(3085 ± 1001 ) ml,t =7.674,P =0.000],stroke volume(SV) [(185 ± 52) ml vs.(114±41)ml,t=7.803,P=0.000],cardiac output (CO)[( 13.9±4.3)L/min vs.(11.2±3.6)L/min,t=4.802,P=0.000],left ventricular end diastolic volume (LVD)[(388± 145)ml vs.(258±98)ml,t =7.673,P =0.000],left ventricular end systolic volume ( LSV ) [( 223 ± 95 ) ml vs.( 135 ± 59) ml,t =7.186,P=0.000] were significantly higher group than in young and middle-aged group.The ejection pressure (EP)[(178±29)mm Hg vs.(183±24)mm Hg,t=2.323,P=0.012],myocardium negative inotropic(MNC) [(0.609±0.149)vs.(0.683±0.188),t=3.113,P=0.002],ejection fraction (EF) [(0.433± 0.034) vs.(0.445 ± 0.031 ),t =2.451,P =0.010],diastolic blood pressure (DBP) [( 87 ±14)mm Hg vs.(1.08±22)mm Hg,t=8.141,P=0.000],systematic vascular resistance(SSR)[(952±207)gcm-4 s-2 vs.(1217± 308) gcm-4 s-2,t =7.143,P=0.000],ejection resistence(ER) [( 178± 29)vs.( 183 ± 24),t =2.323,P =0.012] were lower in elderly group than in young and middle-aged group.DBP(x2 =16.474,P=0.000,OR=0.752,95％CI:0.714-0.790),SBP(x2 =11.913,P=0.000,OR=1.148,95％CI:1.091-1.205),ER(x2 =17.892,P=0.000,OR=0.906,95％CI:0.861-0.951),CVP(x2 =14.672,P=0.000,OR=0.698,95％CI:0.663-0.733) and LDV(x2 =21.080,P=0.000,OR=0.942.95％ CI:0.895-0.989) were dangerous factors of uremia complicating heart failure.Conclnsions The increased volume load,decreased myocardial contractility and cardiac afterload may appear in the elderly patients with uremia complicating heart failure.

We aimed to obtain the recombinant aminopeptidase encoded by Listeria monocytogenes (L. monocytogenes) gene lmo1711, and characterized the enzyme. First, the amino acid sequences of Lmo1711 from L. monocytogenes EGD-e and its homologues in other microbial species were aligned and the putative active sites were analyzed. The putative model of Lmo1711 was constructed through the SWISS-MODEL Workspace. Then, the plasmid pET30a-Lmo1711 was constructed and transformed into E. coli for expression of the recombinant Lmo1711. The his-tagged soluble protein was purified using the nickel-chelated affinity column chromatography. With the amino acid-p-nitroaniline as the substrate, Lmo1711 hydrolyzed the substrate to free p-nitroaniline monomers, whose absorbance measured at 405 nm reflected the aminopeptidase activity. The specificity of Lmo1711 to substrates was then examined by changing various substrates, and the effect of metal ions on the catalytic efficiency of this enzyme was further determined. Based on the bioinformatics data, Lmo1711 is a member of the M29 family aminopeptidases, containing a highly conserved catalytic motif (Glu-Glu-His-Tyr-His-Asp) with typical structure arrangements of the peptidase family. The recombinant Lmo1711 with a size of about 49.3 kDa exhibited aminopeptidase activity and had a selectivity to the substrates, with the highest degree of affinity for leucine-p-nitroaniline. Interestingly, the enzymatic activity of Lmo1711 can be activated by Cd²⁺, Zn²⁺, and is strongly stimulated by Co²⁺. We here, for the first time demonstrate that L. monocytogenes lmo1711 encodes a cobalt-activated aminopeptidase of M29 family.