微电解-水解-好氧工艺处理硝基苯废水

采用微电解－水解－好氧工艺进行了硝基苯废水（COD为1200－1600mg.L^-1，色度为300－400倍）处理的试验研究，结果表明：该工艺可有效地去除硝基苯废水中的有机物和色度，COD和色度的总去除率分别达到90％，85％以上，出水水质符合《污水综合排放标准（GB8978－1996）》中二级标准的排放要求。     

利福霉素生产废水的生物处理

利用投菌法技术，采用水解－流化床－接触氧化工艺处理高浓度利福霉素废水，结果表明COD去除率在96％以上，各项指标达到国家GB978－1996排放标准。     

水解酸化法预处理制药废水的研究

采用水解酸化法对制药废水进行了预处理的研究。结果表明:水解酸化阶段初始COD越大,其最佳HRT越长及COD去除率越低。初始COD为4250mg/L时,BOD/COD达到了0.84,可生化性提高了55%;对于初始COD为9775mg/L的制药废水,BOD/COD的初始值就很高,水解酸化阶段对其可生化性的提高并不明显。对于进水COD为4250mg/L的制药废水,当HRT为12h时,系统达到临界酸化时间。     

无机膜——厌氧水解——SBR好氧工艺在油脂洗涤废水中的应用

介绍一种新的处理油脂洗涤废水的工艺流程－－无机膜－－厌氧水解－－SBR好氧工艺。通过无机膜在油脂洗涤废水处理中的应用，有效降低了废水的进水浓度，同时结合运用改进的生化处理方法－－SBR法，确保废水排放稳定达标，解决了油脂废水处理中的难题。     

水解酸化—Fenton试剂氧化处理牛仔服装洗水废水试验研究

采用水解酸化—Fenton试剂组合工艺对某牛仔制衣厂洗水废水进行处理。确定了水解酸化最佳反应时间为8h,考察了硫酸亚铁投加量、双氧水投加量、反应时间及pH值对洗水废水的色度及COD去除率的影响,通过正交实验确定了Fenton试剂处理该废水的最佳操作条件为:反应时间30min、双氧水(30%)投加量4mL/L、硫酸亚铁投加量300mg/L、pH值为4左右。在最佳条件下,色度与COD去除率分别达到95%和88%以上,出水COD值为145mg/L左右,水质澄清,符合GB 8978—1996《污水综合排放标准》中的二级标准,可达标排放。     

从空间与时间上分析我国餐饮业的地理集聚特征

介绍了采用A1-A2-O-M工艺处理焦化废水A1-A2段COD的去除特性,并得出了两段反应器各自的最佳运行控制参数,包括进水pH值、温度、进水COD浓度、水力停留时间等,通过试验,证实了厌氧水解酸化对焦化废水可生化性的提高有明显作用,BOD5/COD从0.348提高到0.440。     

焦化废水A1-A2-O-M工艺A1-A2段COD去除特性研究

介绍了采用A1-A2-O-M工艺处理焦化废水A1-A2段COD的去除特性,并得出了两段反应器各自的最佳运行控制参数,包括进水pH值、温度、进水COD浓度、水力停留时间等,通过试验,证实了厌氧水解酸化对焦化废水可生化性的提高有明显作用,BOD5/COD从0.348提高到0.440。     

水解酸化-好氧处理石油化工废水试验研究

试验采用水解酸化接好氧工艺处理石化废水 ,水解酸化池停留时间 1 5h ,后接 1 0h左右的好氧处理 ,COD去除率可以达到 90 %以上 ,BOD去除率达到 90 %以上 .通过考察水解酸化 -好氧系统对CODCr、BOD5的去除效果 ,分析了系统中COD、BOD去除情况 ,并分析了污泥具有良好絮凝沉降性能的原因     

包装印刷废水处理工程

本文采用混凝沉淀-水解酸化-生物接触氧化组合工艺处理包装印刷废水,取得了很好的处理效果,其对废水中COD、SS、色度等污染指标的去除率均在95%以上。     

催化铁内电解-A/O工艺处理压缩机生产废水

采用催化铁内电解-A/O工艺处理压缩机生产混合废水.实验结果表明,催化铁内电解对混合废水中COD的去除率达到了35%左右,TP去除率超过98%,BOD5/COD由0.18提高至0.30以上.催化铁内电解出水经水解酸化,BOD5/COD进一步提高至0.45.组合工艺系统COD、悬浮物SS、总磷TP去除率分别达到93%,94%和99%以上.     

Cyclin is degraded by the ubiquitin pathway.

Cyclin degradation is the key step governing exit from mitosis and progress into the next cell cycle. When a region in the N terminus of cyclin is fused to a foreign protein, it produces a hybrid protein susceptible to proteolysis at mitosis. During the course of degradation, both cyclin and the hybrid form conjugates with ubiquitin. The kinetic properties of the conjugates indicate that cyclin is degraded by ubiquitin-dependent proteolysis. Thus anaphase may be triggered by the recognition of cyclin by the ubiquitin-conjugating system.     

泛素调节的蛋白质降解--2004年诺贝尔化学奖成果简介

以色列科学家阿龙·切哈诺沃(Aaron Ciechanover)、阿夫拉姆·赫什科(Avram Hershko)和美国科学家欧文·罗斯(Irwin Rose)因发现泛素调节的蛋白质降解被授予2004年诺贝尔化学奖.泛素是一种含76个氨基酸的多肽,存在于除细菌外的许多不同组织和器官中,具有标记待降解蛋白质的作用.被泛素标记的蛋白质在蛋白酶体中被降解.泛素控制的蛋白质降解具有重要的生理意义,它不仅能够清除错误蛋白质,对细胞生长周期、DNA复制以及染色体结构都有重要的调控作用.     

苹果受粉前后子房的生化变化

本文报道了苹果受粉前后子房内Ｐｒ／ＲＮＡ、蛋白水解酶活性及过氧化物同工酶的变化．花开后６ｄ，受粉子房Ｐｒ／ＲＮＡ维持在较高水平，未受粉子房则是在花开３ｄ时比值升高，到６ｄ时该比值又降低；蛋白水解酶活性的变化相似于Ｐｒ／ＲＮＡ值在上述两种材料中的变化情况；与未受粉子房相比，受粉子房在受粉后新出现了两条大分子量的过氧化物同工酶带．本文还对受粉与否所引起不同的发育途径及蛋白水解酶活性、过氧化物同工酶变化与子房发育的关系作了初步探讨．     

Differential expression of calmodulin-binding proteins in B, T lymphocytes and thymocytes

Changes in intracellular free Ca2+ are involved in the transmembrane signalling of different cells, including lymphocytes. Since calmodulin (CaM) is a primary receptor for Ca2+ (ref. 4), it may mediate the activation of crucial enzymes after antigen-induced increases in cytosolic Ca2+. Using a biotinylated-CaM (Bio-CaM) detection procedure to identify such proteins, we found that a peptide of relative molecular mass 59,000 (59K) was the predominant soluble CaM-binding protein (CaM-BP) in T cells and B lymphocytes from murine spleen; immunoblotting experiments identified it as a subunit of the CaM-dependent phosphatase, 'calcineurin' (CN). Smaller amounts of larger CaM-BPs, thought to be cytoskeletal-binding proteins, were also detected. CaM-BPs were expressed differentially, with B lymphocytes having four times more of the CN-like protein than T lymphocytes, while in thymocytes, a 65K polypeptide was the major CaM-BP. However, limited proteolysis analysis suggested that this thymus-specific peptide may be a precursor of CN. These data suggest that Ca2+-stimulated protein dephosphorylation may be an important and highly regulated function in lymphoid cells.     

Plakalbumin, alpha 1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosis

An old puzzle in protein biochemistry concerns the ready conversion of ovalbumin, by proteolysis, to the much more stable derivative, plakalbumin. Ovalbumin is now known to belong to the serpin superfamily, most of which are serine proteinase inhibitors. We report here studies of two such members of the family, the human plasma proteins alpha 1-antitrypsin and antithrombin, and show that they undergo a similar change in stability on selective proteolysis. This change, which is accompanied by a loss of inhibitory activity, can best be considered as an irreversible molecular transition from a native stressed (S) conformation, to a more ordered relaxed (R) form. The maintenance of the native S conformation, and hence the maintenance of inhibitory activity, is critically dependent on the integrity of an exposed loop of polypeptide. We propose that the susceptibility of this peptide loop to proteolytic cleavage gives it an incidental role as a physiological switch which allows the inactivation of individual inhibitors by specific proteolysis. The vulnerability of this exposed loop in each inhibitor also explains the pathological action of a number of venoms and toxins. In particular, the demonstration here of the cleavage of antithrombin, by leukocyte elastase, explains an observed change in blood coagulation that accompanies severe inflammation and which can result in fatal thrombosis.     

Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination.

Ornithine decarboxylase (ODC), a key enzyme in polyamine biosynthesis, is the most rapidly turned over mammalian enzyme. We have shown that its degradation is accelerated by ODC antizyme, an inhibitory protein induced by polyamines. This is a new type of enzyme regulation and may be a model for selective protein degradation. Here we report the identification of the protease responsible for ODC degradation. Using a cell-free degradation system, we demonstrate that immunodepletion of proteasomes from cell extracts causes almost complete loss of ATP- and antizyme-dependent degradation of ODC. In addition, purified 26S proteasome complex, but not the 20S proteasome, catalyses ODC degradation in the absence of ubiquitin. These results strongly suggest that the 26S proteasome, widely viewed as specific for ubiquitin-conjugated proteins, is the main enzyme responsible for ODC degradation. The 26S proteasome may therefore have a second role in ubiquitin-independent proteolysis.     

Proteolysis, proteasomes and antigen presentation.

Proteins presented to the immune system must first be cleaved to small peptides by intracellular proteinases. Proteasomes are proteolytic complexes that degrade cytosolic and nuclear proteins. These particles have been implicated in ATP-ubiquitin-dependent proteolysis and in the processing of intracellular antigens for cytolytic immune responses.     

Probing the Proteolysis of Melitin Using Liquid Secondary Ion Mass Spectrometry

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Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication.

SCF ubiquitin ligases target phosphorylated substrates for ubiquitin-dependent proteolysis by means of adapter subunits called F-box proteins. The F-box protein Cdc4 captures phosphorylated forms of the cyclin-dependent kinase inhibitor Sic1 for ubiquitination in late G1 phase, an event necessary for the onset of DNA replication. The WD40 repeat domain of Cdc4 binds with high affinity to a consensus phosphopeptide motif (the Cdc4 phospho-degron, CPD), yet Sic1 itself has many sub-optimal CPD motifs that act in concert to mediate Cdc4 binding. The weak CPD sites in Sic1 establish a phosphorylation threshold that delays degradation in vivo, and thereby establishes a minimal G1 phase period needed to ensure proper DNA replication. Multisite phosphorylation may be a more general mechanism to set thresholds in regulated protein-protein interactions.     

Relative proteolysis of the fibrinogen B beta chain by thrombin and plasmin as a determinant of thrombosis

Thrombosis results, in part, from localized accumulation of fibrin, implying an imbalance between its rate of formation and dissolution. Astrup postulated that patency of the vascular system depended on a dynamic equilibrium between constantly active coagulation and fibrinolytic systems. Reviews of this hypothesis have concluded that neither thrombin nor plasmin proteolysis makes a major contribution to fibrinogen turnover in normal individuals and that the hypothesis of a dynamic equilibrium between clotting and lysis remains unproven. Thus, the current view is that plasmin simply serves the function of a fibrinolytic enzyme digesting fibrin in the vascular system. Here, I promote the alternative view that the relative rates of proteolysis of the B beta chain of fibrinogen by thrombin and plasmin determine the occurrence of thrombosis. This view is supported by recent data and can be used to make some readily testable predictions.