蝮蛇抗栓酶对家兔慢性胆囊炎防治的实验研究

作者用家兔４２只随机分成造型组（Ａ）,预防组（Ｂ）及治疗组（Ｃ）。各组又分处理组（Ａ１、Ｂ１、Ｃ１）和对照组（Ａ２、Ｂ２、Ｃ２）两个亚组。Ａ２组仅喂基本饲料,其余５组喂基本饲料加造型剂。Ａ组没用任何治疗。Ｂ１组慢性胆囊炎形成前,Ｃ１组慢性胆囊炎形成后分别用蝮蛇抗栓酶（０．２Ｕ／ｋｇ／日３０天）,Ｂ２和Ｃ２组仅给等量生理盐水。Ａ２及治疗后的Ｂ１、Ｃ１组血清胆固醇含量均明显低于Ａ１、Ｂ２、Ｃ２组（Ｐ＜０．０５）。胆囊的病理变化,Ｂ２和Ｃ２组改变明显,表面呈暗褐色,与周围组织粘连,粘膜面粗糙,胆囊壁增厚,体积增加,胆汁潴留,镜下粘膜增生呈乳头状,部分粘膜脱落,粘膜下及肌层水肿,炎细胞浸润。结果表明,蝮蛇抗栓酶对慢性胆囊炎既有预防作用又有治疗作用。     

双酶法制备玉米皮膳食纤维的研究

采用蛋白酶和淀粉酶结合水解制备玉米皮膳食纤维,通过正交试验确立了玉米皮膳食纤维的双酶法制备工艺。双酶法制备的玉米皮膳食纤维的产率为59.4%,膳食纤维的蛋白质量分数为0.82%,淀粉质量分数为1.42%,灰分为0.4%,水分质量分数为8.6%,持水力为5.9±0.4 g.g-1。     

Effects of Water on Enzyme Performance with an Emphasis on the Reactions in Supercritical Fluids

ABSTRACT

Enzymes require a certain level of water in their structures in order to maintain their natural conformation, allowing them to deliver their full functionality. Furthermore, as a modifier of the solvent, up to a certain level, water can modify the solvent properties such as polarity/polarizability as well as the solubility of the reactants and the products. In addition, depending on the type of the reaction, water can be a substrate (e.g., in hydrolysis) or a product (e.g., in esterolysis) of the enzymatic reaction, influencing the enzyme turnover in different ways. It is found that regardless of the type of reaction, the functionality of enzyme itself is maximum at an optimum level of water, beyond which the enzyme performance is declined due to the loss in enzyme stability. Furthermore, mass transfer limitations caused by pathway blockage and/or by reduced solubilities of the reactants and/or products can also affect the enzyme performance at higher water levels. Controlling water content of ingoing CO₂ and substrates as well as precise management of enzyme support and salt hydrates are important strategies to adjust water level in reaction media, especially in supercritical environments.     

蝮蛇抗栓酶治疗急性心肌梗塞疗效与剂量,时间的关系

用蝮蛇抗栓酶治疗急性心肌梗塞６２例,按用药剂量及治疗时间各分成２组对比,结果表明在急性心肌梗塞早期（８ｈ内）使用大剂量蝮蛇抗栓酶（＞２ＩＵ）,治疗效果较明显且病死率明显降低（Ｐ＜０．０５）。     

低温酶及其冷适应性机制研究进展

生活在极地、深海等常年低温环境中的低温微生物和部分变温生物,能够通过产生低温酶来适应在低温环境中的生长、繁殖和代谢。这些酶在低温或常温条件下具有很高的催化活性,对热却很敏感,在高温时能够快速失活,因此在实际的生产和生活中具有广泛的应用前景。基于这些特性,低温酶的冷适应性机制研究成为了当前的一个热点。较系统地综述了低温酶的来源、特点、生产状况以及具有代表性的几种低温酶的冷适应性机制。     

Autoinhibition Mechanism of the Ubiquitin-Conjugating Enzyme UBE2S by Autoubiquitination

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猪苓及猪苓多糖对BBN联合糖精作用Fisher-344大鼠肝脏代谢酶的影响

以BBN联合糖精作用Fisher-344大鼠,分别使用ELISA及RT-PCR方法测定样本中CYP450、GST和NQO1酶活性及Gstpi和NQO1 mRNA相对表达含量。结果表明,猪苓及猪苓多糖均可使样本中CYP450酶活性显著降低,其中猪苓对CYP450酶活性抑制呈剂量依赖性;猪苓及猪苓多糖对样本中GST无明显影响,猪苓可显著升高样本中NQO1酶活性;猪苓高剂量及猪苓多糖可上调GSTPi mRNA表达,猪苓及猪苓多糖对NQO1 mRNA表达无明显作用。研究表明猪苓及猪苓多糖抗癌作用与降低CYP450与升高NQO1酶活性有关,但机制有待进一步研究。     

Cleavage of individual DNA strands by the different subunits of the heterodimeric restriction endonuclease BbvCI

BbvCI cleaves an asymmetric DNA sequence, 5'-CC downward arrow TCAGC-3'/5'-GC downward arrow TGAGG-3', as indicated. While many Type II restriction enzymes consist of identical subunits, BbvCI has two different subunits: R(1), which acts at GC downward arrow TGAGG; and R(2), which acts at CC downward arrow TCAGC. Some mutants of BbvCI with defects in one subunit, either R(1)(-)R(2)(+) or R(1)(+)R(2)(-), cleave only one strand, that attacked by the native subunit. In analytical ultracentrifugation at various concentrations of protein, wild-type and mutant BbvCI enzymes aggregated extensively, but are R(1)R(2) heterodimers at the concentrations used in DNA cleavage reactions. On a plasmid with one recognition site, wild-type BbvCI cleaved both strands before dissociating from the DNA, while the R(1)(-)R(2)(+) and R(1)(+)R(2)(-) mutants acted almost exclusively on their specified strands, albeit at relatively slow rates. During the wild-type reaction, the DNA is cleaved initially in one strand, mainly that targeted by the R(1) subunit. The other strand is then cleaved slowly by R(2) before the enzyme dissociates from the DNA. Hence, the nicked form accumulates as a transient intermediate. This behaviour differs from that of many other restriction enzymes, which cut both strands at equal rates. However, the activities of the R(1)(+) and R(2)(+) subunits in the wild-type enzyme can differ from their activities in the R(1)(+)R(2)(-) and R(1)(-)R(2)(+) mutants. Each active site in BbvCI therefore influences the other.