双环醇片治疗慢性肝炎高转氨酶血症的疗效观察

目的：观察双环醇片治疗慢性肝炎高转氨酶血症的临床疗效。方法：选择住院或门诊慢性肝炎高转氨酶血症患者280例,随机分为治疗组和对照组,治疗组141例,对照组139例。治疗组在常规保肝治疗的基础上加用双环醇片25m每日3次口服,对照组在常规保肝治疗的基础上加用甘利欣胶囊150mg每日3次口服。疗程均为4周。治疗前后每周详细记录患者症状、体征、肝功能、肾功能、电解质、及血尿常规,同时记录治疗过程中的不良反应及停药后随访3个月。结果：两组均有显著疗效,肝功能生化指标与治疗前相比有显著性差异（治疗组P〈0.01,对照组P〈0.05）,治疗组明显优于对照组（P〈0.05）,且治疗组出现的不良反应明显少于对照组。结论：双环醇片治疗慢性肝炎高转氨酶血症疗效好,不良反应较少,值得临床推广。     

源首胶囊治疗新生儿高胆红素血症疗效观察

目的及早有效地纠正新生儿高胆红素血症,预防胆红素脑损伤。方法将98例患儿随机分为2组。治疗组在常规治疗的同时加用源首胶囊口服。结果出院时治疗组胆红素含量(60.23±34.82)μm o l/L,明显低于对照组(89.47±36.76)μm o l/L(P<0.05);治愈天数治疗组(5.23±1.62)d明显低于对照组(6.92±1.79)d(P<0.01)。结论源首胶囊治疗新生儿高胆红素血症,可迅速降低血胆红素水平,明显缩短治疗时间,且安全性高,无副作用。     

蝮蛇抗栓酶胶囊治疗高粘血症187例疗效观察

1998年以来 ,我院应用蝮蛇抗栓酶胶囊 (下称抗栓酶胶囊 )治疗高粘血症 1 87例 ,疗效显著 ,现总结报告如下。1　临床资料1 .1　一般资料　本组 1 87例均为门诊病人 ,其中男 1 3 2例 ,女 5 5例 ;年龄 3 9～ 74岁 ,其中年龄 3 9～ 49岁 78例 (4 1 .7% ) ,5 0～ 69岁 85例 (4 5 .5 % ) ,70岁以上 2 4例 (1 2 .8% ) ;病程最短 3个月 ,最长3年 ,多为长时间服用其它药物无效者。其中有脑动脉硬化 78例 ,有高血压病史 1 2 5例 ,有冠心病2 5例。均经查血液流变学检测确诊。1 .2　治疗方法　应用蝮蛇抗栓酶 0 .5～ 0 .75 u (2～ 3支 )改装入肠溶胶囊中…     

富马酸替诺福韦二吡呋酯片联合双环醇在治疗慢性乙型病毒性肝炎方面的研究

目的:研究探讨富马酸替诺福韦二吡呋酯片(tenofovir dipivoxil fumarate tablets,TDF)联合双环醇在治疗慢性乙型病毒性肝炎方面的临床效果.方法:选取2017年1月-2020年1月中国人民解放军陆军第七十三集团军医院疾病预防控制科感染病区收治的80例慢性乙型病毒性肝炎患者,随机将其分为两...     

胆红素血浆吸附治疗高胆红素血症疗效观察

我院1999年10月至2003年12月先后对32例高胆红素血症的重型肝炎患者进行胆红素血浆吸附治疗,在加快黄疸消退,提高患者生存率方面取得了较好的效果.现报告如下.     

降纤酶治疗高粘血症40例报告

目的：观察降纤酶治疗高粘血症患者的临床疗效。方法用生理盐水２５０ｍｌ加降纤酶５ｕ,体重超过６５ｋｇ和１０ｕ,静脉滴注,每天１次,连用３天,第４天停用,第５天开始隔天静脉滴注降纤酶５ｕ或者１０ｕ,总量６０ｕ。结果降纤酶能明显地降低高粘血症患者的血液粘度、纤维蛋白原、红细胞聚集指数、微循环滞留时间等,同时也能使患者原有临床症状和体征以及微循环得到明显改善,结论降纤酶是治疗高粘血症的有效药物。     

中药大黄敷脐治疗新生儿高胆红素血症的临床观察

目的观察中药大黄敷脐治疗新生儿高胆红素血症的临床疗效。方法将100例高胆红素血症新生儿随机分为观察组和对照组,对照组50例采取常规治疗,观察组50例在常规治疗基础上加用中药大黄敷脐。结果两组患儿治疗前胆红素值比较无统计学意义(P0.05);治疗后两组患儿每天胆红素下降值、降至正常范围所需时间比较,差异有统计学意义(P0.05)。结论在常规治疗基础上加用中药大黄敷脐治疗新生儿高胆红素血症可迅速降低血清胆红素水平,疗效显著,是一种可靠的治疗方法。     

阿托伐他汀钙片对高胆固醇血症的降脂疗效的临床观察

本文主要通过对高胆固醇血症患者进行不则剂量的阿托伐他汀钙片分组治疗,从而验证不同剂量的阿托伐他汀钙片对高胆固醇血症的降脂疗效,实验结果显示较高剂量(60mg/日)的阿托伐他汀钙片对高胆固醇血症的治疗具有较理想的效果。     

金双歧治疗新生儿高胆红素血症的临床疗效研究

目的 探讨微生态制剂金双歧(双歧杆菌乳酸杆菌三联活菌片)对新生儿高胆红素血症的临床疗效,以找出能及早有效地纠正新生儿高胆红素血症,预防新生儿胆红素脑病发生的新方法.方法 通过随机抽样、收集青白江区人民医院2007年3月至2011年3月72例新生儿高胆红素血症患儿的临床资料并进行回顾性分析,将72例新生儿高胆红素血症患儿随机分为治疗组40例和对照组32例.对照组给予常规治疗,治疗组在常规治疗基础上,加用金双歧1片(0.5亿)/次,每天3次,温开水溶碎后喂服或经胃管注入,共7～10d.检测治疗前后两组血清胆红素水平、计算日平均经皮测胆红素下降值、平均住院时间和黄疸消退时间.结果 金双歧辅助治疗新生儿高胆红素血症,治疗后治疗组与对照组血清总胆红素水平分别为(58.21 +4.36) μmol/L和(64.16±5.29) μmol/L(P ＜0.01);治疗组和对照组日平均经皮测胆红素下降值、平均住院时间和黄疸退尽平均时间分别为( 10.35±2.46)、(7.68±1.35)μmol/L;( 6/54±2/59)、(9/05 +3/12)d; (6/38±1/38)、( 8/75±2/68)d;差异均有统计学意义(P＜0.01).结论 应用金双歧治疗新生儿高胆红素血症可迅速降低血胆红素水平,缩短治疗时间,预防胆红素脑病的发生疗效确切、安全,可作为治疗新生儿高胆红素血症的方法之一,值得临床应用推广.     

中药当归枸杞子汤调节高泌乳素血症临床观察

目的通过连续动态监测泌乳素血液浓度,评价当归枸杞子汤对高泌乳素血症的调节作用。方法选择我院2012年5月~2013年5月门诊收治的高泌乳素血症患者130例,随机分为对照组30例,采用溴隐亭治疗;观察组100例,给予中药当归枸杞子汤治疗。连续动态监测血清泌乳素浓度,评价两组疗效。结果两组患者疗效比较无显著统计学意义(P0.05)。两组治疗后血清泌乳素均显著下降,与治疗前比较差异有统计学意义(P0.05);而两组治疗后比较差异无统计学意义(P0.05)。不良反应发生率比较,对照组显著高于观察组(P0.05)。结论中药当归枸杞子汤治疗高泌乳素血症安全、有效,且价格低廉,用法简单,有显著的临床推广应用价值。     

The clinical chemistry of chimpanzees. I. Determination of aminotransferase baseline values for hepatitis studies

Viral hepatitis in chimpanzees produces negligible symptomatology, and serum aminotransferase changes may be minimal. To maximize the predictive value of these determinations, which are the only serum indicators available for non-A non-B (NANB) hepatitis infection, normal ranges for aspartate and alanine aminotransferases (AST, ALT) were examined and categorized according to age and sex. Males were found to have higher values than females, and adults higher values than juveniles. The kinetic method used and the values obtained are described. Differences in methodologies and reporting units are discussed.     

Bicyclol: a novel antihepatitis drug with hepatic heat shock protein 27/70-inducing activity and cytoprotective effects in mice

Heat shock proteins (HSPs) are the best-known endogenous factors that protect against cell injury under various pathological conditions and that can be induced by various physical, chemical, and biological stressors. New research seeks to discover a compound that is clinically safe and can induce the accumulation of HSPs in patients. This paper reports that the oral administration of three doses of bicyclol, a novel antihepatitis drug, induced hepatic HSP27 and HSP70 expression in a time- and dose-dependent manner, and that bicyclol treatment stimulated heat shock factor 1 (HSF1) activation in mice. The inducing effects of bicyclol on HSP27, HSP70 and HSF1 were all blocked by quercetin, an inhibitor of HSP biosynthesis. The cytoprotective effect of HSP27/70 induced by bicyclol against hepatotoxicity of acetaminophen (AP) was assessed in mice. The prior administration of bicyclol markedly suppressed AP-induced liver injury as indicated by the reduction in the elevation of serum alanine aminotransferase and aspartate aminotransferase, in liver necrosis, in the release of cytochrome c and apoptosis-inducing factor from mitochondria, as well as in hepatic deoxyribonucleic acid fragmentation in mice. However, all the above actions of bicyclol against AP-induced mouse liver injuries were significantly attenuated by quercetin. This is the first report to show that bicyclol induces hepatic HSP27/70 expression via activation of HSF1 and that the cytoprotective action of bicyclol against liver injury is mediated by its induction of HSP27/70. These results provide new evidence for elucidating the mechanism of the hepatoprotective action of bicyclol in animals and patients.     

Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis.

Although several high-resolution X-ray crystallographic structures have been determined for Escherichia coli aspartate aminotransferase (eAATase), efforts to crystallize E. coli tyrosine aminotransferase (eTATase) have been unsuccessful. Sequence alignment analyses of eTATase and eAATase show 43% sequence identity and 72% sequence similarity, allowing for conservative substitutions. The high similarity of the two sequences indicates that both enzymes must have similar secondary and tertiary structures. Six active site residues of eAATase were targeted by homology modeling as being important for aromatic amino acid reactivity with eTATase. Two of these positions (Thr 109 and Asn 297) are invariant in all known aspartate aminotransferase enzymes, but differ in eTATase (Ser 109 and Ser 297). The other four positions (Val 39, Lys 41, Thr 47, and Asn 69) line the active site pocket of eAATase and are replaced by amino acids with more hydrophobic side chains in eTATase (Leu 39, Tyr 41, Ile 47, and Leu 69). These six positions in eAATase were mutated by site-directed mutagenesis to the corresponding amino acids found in eTATase in an attempt to redesign the substrate specificity of eAATase to that of eTATase. Five combinations of the individual mutations were obtained from mutagenesis reactions. The redesigned eAATase mutant containing all six mutations (Hex) displays second-order rate constants for the transamination of aspartate and phenylalanine that are within an order of magnitude of those observed for eTATase. Thus, the reactivity of eAATase with phenylalanine was increased by over three orders of magnitude without sacrificing the high transamination activity with aspartate observed for both enzymes.(ABSTRACT TRUNCATED AT 250 WORDS)     

Inhibition of aspartate aminotransferase by hydrazinosuccinate

DL-Hydrazinosuccinic acid was synthesized by the reaction of DL-bromosuccinic acid with hydrazine. The compound strongly inhibited aspartate aminotransferase and gave 50% inhibition at 1.3 μM when added simultaneously with L-aspartate to an assay mixture containing enzyme. Incubation of the enzyme with the compound prior to assay resulted in a much stronger inhibition, which proceeded time-dependently. The inhibition was protectable with L-aspartate and was substantially reversed by dialysis.     

The three-dimensional structure of mitochondrial aspartate aminotransferase at 4.5 A resolution

An X-ray crystallographic study at 4.5 Å resolution has been carried out with triclinic crystals of chicken mitochondrial aspartate aminotransferase.In the electron density map, the enzyme is clearly visible as an isologous α₂-dimer (105 Å × 60 Å × 50 Å) in which the subunits are associated about a molecular 2-fold axis. Each subunit of dimensions 70 Å × 50 Å × 40 Å contains at least seven helices, one of which is about 50 Å long.Difference maps have revealed the positions of the pyridoxyl and the phosphate moieties of the coenzyme as well as the general substrate binding area. The active sites are on opposite sides of the dimer, about 30 Å apart and close to the intersubunit boundary, so that probably both subunits contribute to each active site. An isolated chain segment, passing in front of the active site and ending in contact with the neighbouring subunit is interpreted as one of the chain termini.     

钝齿棒杆菌N-乙酰鸟氨酸转氨酶的克隆表达分析及其重组菌的精氨酸发酵

N-乙酰鸟氨酸转氨酶 (EC 2.6.1.11,ACOAT) 是钝齿棒杆菌Corynebacterium crenatum精氨酸合成途径中的第4个酶,催化底物N-乙酰谷氨酸半醛生成产物N-乙酰鸟氨酸。为研究N-乙酰鸟氨酸转氨酶在钝齿棒杆菌中精氨酸合成中的作用,考察其酶学性质,对培养基成分和发酵过程工艺条件的优化提高精氨酸产量提供依据。从精氨酸高产菌株钝齿棒杆菌SYPA 5-5染色体扩增获得ACOAT编码基因argD,全长1 176 bp,编码390个氨基酸,在Escherichia coli BL21(D     

Purification and properties of alanine aminotransferase from maize (Zea mays L.) leaves

Alanine aminotransferase (AlaAT, EC 2.6.1.2) from leaves of 14-day-old maize seedlings was purified over 1600-fold to electrophoretical homogeneity. Specific activity of the purified enzyme measured with L-alanine and 2-oxoglutarate as substrates was 2125 nkat·(mg protein)⁻¹ at 30 °C. The molecular weights of the native and sodium dodecyl sulfate — denatured AlaAT protein were 95 kDa and 50 kDa respectively, indicating that the native enzyme is probably a homodimer. AlaAT almost exclusively catalyzed amino group transfer from L-alanine to 2-oxoglutarate and the reverse reaction. The inhibitory experiments showed that pirydoxal phosphate is directly involved in the enzymatic catalysis and the enzyme molecule contains essential SH groups. The use of phenylglyoxal demonstrated the presence of arginine residue as anionic binding site in the active centre of AlaAT. This work was supported by the State Committee for Scientific Research, a grant No. 5PO6A00510     

Properties of serine：glyoxylate aminotransferase purified from Arabidopsis thaliana leaves

The photorespiratory enzyme L-serine：glyoxylate amino- transferase （SGAT; EC 2.6.1.45） was purified from Arabidopsis thaliana leaves. The f＇mal enzyme was approximately 80 % pure as revealed by sodium dodecyl sulfatepolyacrylamide gel electrophoresis with silver staining. The identity of the enzyme was confirmed by LC/MS/MS analysis. The molecular mass estimated by gel filtration chromato- graphy on Sephadex G-150 under non-denaturing conditions, mass spectrometry （matrix-assisted laser desorption/ ionization/time of flight technique） and sodium dodecyl sulfate-polyacrylamide gel electrophoresis was 82.4 kDa, 42.0 kDa, and 39.8 kDa, respectively, indicating dimer as the active form. The optimum pH value was 9.2. The enzyme activity was inhibited by aminooxyacetate and β-chloro-L-alanine both compounds reacting with the carbonyl group of pyridoxal phosphate. The enzyme＇s transaminating activity with L-alanine and glyoxylate as substrates was approximately 55 % of that observed with L-serine and glyoxylate. The lower Kmvalue （1.25 mM） for L-alanine, compared with that of other plant SGATs, and the kcat/Km（Ala） ratio being approxi- mately 2-fold higher than kcat/Km（Ser） suggested that, during photorespiration, Ala and Ser are used by Arabidopsis SGAT with equal efficiency as amino group donors for glyoxylate. The equilibrium constant （Keq）, derived from the Haldane relation, for the transamination reaction between L-serine and glyoxylate with the formation of hydroxypyruvate and glycine was 79.1, strongly favoring glycine synthesis. However, it was accompanied by a low Km value of 2.83 mM for glycine. A comparison of some kinetic properties of the studied enzymes with the recombinant Arabidopsis SGATs previously obtained revealed substantial differences. The ratio of the velocity of the transamination reaction with L-alanine and glyoxylate as substrates versus that with L-serine and glyoxylate was 1：1.8 for the native enzyme, whereas it was 1：7 for the recombinant SGAT. Native SGAT showed a much lower Km value for L-alanine compared to the recombinant enzyme.