裂果易发性不同的荔枝品种果皮中细胞壁代谢酶活性的比较

“糯米糍”荔枝裂果率极显著高于“淮枝”,前者果皮中的果胶酶、纤维素酶和果胶甲酯酶的活性高于后者,其中以果胶酶活性差异最明显,其次是纤维素酶,果胶甲酯酶差异最小;“糯米糍”细胞壁结合型的过氧化物酶(POD)和多酚氧化酶(PP0)活性明显高于“淮枝”,而水溶性POD和PP0的活性则两个品种间无明显差异。据此认为,果皮细胞壁水解酶活性以及细胞壁结合型的POD和PPO的活性高的荔枝品种,其裂果率也高。文章对细胞壁代谢相关酶类在果皮抗裂性形成中的作用进行了讨论。     

甘露醇和6—BA处理对水稻细胞过氧化物酶及IAA氧化酶活性的影响

研究了甘露醇和６０ＢＡ处理对水稻服浮细胞再分化、过氧化物酶及ＩＡＡ氧化酶的影响。结果表明,甘露醇处理能延迟水稻细胞衰老,提高细胞再分化能力,降低细胞过氧化物酶和ＩＡＡ氧化酶活性,６－ＢＡ（２ｍｇ／Ｌ）虽然明显降低细胞过氧化物酶活性,但对ＩＡＡ氧化酶及细胞衰老无明显影响,讨论了过氧化物酶及ＩＡＡ氧化酶在水稻胚性细胞形成上的可能作用。     

不同抗性猕猴桃品种感染溃疡病前后几种保护酶活性变化

研究了不同猕猴桃品种展叶孕蕾期自然感染溃疡病菌前后一年生枝条、叶片内过氧化物酶(POD)、多酚氧化酶(PPO)、超氧化物歧化酶(SOD)、过氧化氢酶(CAT)、苯丙氨酸解氨酶(PAL)酶活性的变化情况.结果表明:感染溃疡病菌前后,抗病品种和感病品种枝条及成叶中防御酶系活性变化规律存在一定的差异.品种未受溃疡病菌感染时,一年生枝条、叶片中的POD、PPO、SOD、CAT酶活性抗病品种的酶活性均低于感病品种.品种自然感染溃疡病菌后,一年生枝条、叶片POD、PPO、SOD、CAT、PAL酶活性均升高,且酶活性的增加幅度是抗病品种中酶活提高倍数高于感病品种.而且这种增量在不同保护酶类以及不同组织部位是有差异的.     

碳源和氮源对彩绒革盖菌Coriolus versicolor木质纤维素酶和木质素酶分泌的影响

研究了彩绒草盖菌在不同碳源和氮源培养基中生长时,对纤维素酶、半纤维素酶、木质素酶（漆酶、多酚氧化酶、愈创木酚氧化酶）分泌的影响。结果表明不同碳源和氮源对酶类的分泌影响很大,富含淀粉的物质能明显促进木质素酶的分泌,而专一性底物（纤维素和半纤维素）对纤维素酶和半纤维素酶有诱导作用,麸皮也能诱导半纤维素酶的产生。     

不同氮沉降水平下两种林型的主要土壤酶活性

模拟研究了天然阔叶红松林和天然次生杨桦林不同氮沉降（0、25和50 kg N·hm^-2·a^-1)水平下土壤酶活性(纤维素酶、多酚氧化酶和蔗糖酶)的变化趋势.结果表明：氮沉降增加对土壤酶活性的作用与林分类型有关,短期施氮可以显著影响土壤酶的活性;高氮沉降降低了土壤多酚氧化酶活性,且随着多酚氧化酶活性的降低,两种林型土壤纤维素酶和蔗糖酶活性也有降低的趋势.     

香荚兰成熟荚果中三种酶的活性测定

不同级别的香荚兰 (Vanillaplanifolia)成熟荚果以及其中的种子和肉质果壳中的 β -葡萄糖甙酶、过氧化物酶和多酚氧化酶的活性研究结果表明高等级的果荚中过氧化物酶活性高于低等级的果荚 ,种子中的 β -葡萄糖苷酶活性几乎达到肉质果荚的 2倍 ;过氧化物酶的活性主要分布在果壳中 ,没有在种子中测过氧化物酶的活性 ;多酚氧化酶的活性在测定样品极低 ,未能测出。     

从几个生理指标探讨不同发育程度切花菊耐藏性的差异

本文从分析切花菊贮藏期间可溶性糖含量、过氧化物酶、过氧化氢酶和多酚氧化酶等酶活性变化动态,探讨不同发育程度采收的切花菊耐藏性差异。研究表明,发育程度较高的切花菊含有较高的可溶性糖。贮藏期间,其过氧化物酶活性较低,过氧化氢酶活性变幅较小,峰值出现较晚,这些可能是引起不同发育期采收切花菊耐藏性差异的原因。     

9个辣椒雄性不育材料花蕾生理生化特性研究

以9个辣椒雄性不育材料及其相应的保持系为试材,对有关花器的植物学性状进行了系统观察和研究,测定了花蕾中过氧化物酶、过氧化氢酶、多酚氧化酶的活性和游离脯氨酸的含量。结果表明:供试9个雄性不育材料和保持系的主要花器性状有一定差异;雄性不育材料的过氧化物酶活性和多酚氧化酶活性均高于相应的保持系, 而过氧化氢酶活性低于保持系;保持系游离脯氨酸含量离于不育材料;所测的3种酶活性和脯氨酸含量在雄性不育材料与保持系间差异显著。     

试管棉纤维发育中IAA氧化酶和POD活性的变化(简报)

试管棉纤维发育过程中,ＩＡＡ氧化酶和过氧化物酶的离子型与壁结合的酶活性和纤维细胞的伸长呈负相关,可溶性酶的活性总趋势和离子型的一致。     

石油污染土壤的生物修复与土壤酶活性关系

研究了不同油浓度污染土壤经过两个为期125d的生物修复后的土壤中过氧化氢酶、多酚氧化酶和脂肪酶的酶活变化,分析了土壤中3种酶活性的变化特征与规律。结果表明,随着油浓度的增加,土壤中过氧化氢酶和多酚氧化酶的活性下降,脂肪酶活性增加;经过生物修复后,土壤中的过氧化氢酶和多酚氧化酶的活性在第二周期要比第一周期提高,而脂肪酶活性下降;这3种土壤酶活性变化受污染物浓度影响不显著,但不同浓度油污染土壤的修复对过氧化氢酶的影响要大于对多酚氧化酶和脂肪酶的影响。     

一株口腔链球菌新种—寡发酵链球菌产过氧化氢特性的研究

从健康人口腔中分离的寡发酵链球菌(Streptococcus oligofermentans)能够产生大量的过氧化氢,可能具有抑制致病菌的潜力。为了研究该细菌产过氧化氢的特性,检测了其在不同生长时期和从不同底物产过氧化氢的能力。结果表明,寡发酵链球菌从对数生长早期就开始产过氧化氢,在对数生长后期及稳定期过氧化氢产量达到最高,随后下降。在PYG培养基中,寡发酵链球菌所产的过氧化氢主要来源于大豆蛋白胨和酵母提取物;而代谢终产物乳酸也可作为过氧化氢产生的底物。对3种可能与过氧化氢生成有关的氧化酶的酶活测定表明,寡发酵链球菌具有乳酸氧化酶(LOX)及NADH氧化酶(NOX)的活性,说明其过氧化氢的产生主要依赖于这两种酶的活力。     

D-Aspartate oxidase and D-amino acid oxidase are localised in the peroxisomes of terrestrial gastropods

D-Aspartate oxidase and D-amino acid oxidase were found in high activity in the tissues of representative species of terrestrial gastropods. Analytical subcellular fractionation demonstrated that both of these oxidases co-localised with the peroxisome markers, acyl-CoA oxidase and catalase, in the digestive gland homogenate. Electron microscopy of peak peroxisome fractions showed particles of uniform size with generally well preserved variably electron-dense matrices bounded by an apparently single limiting membrane. Many of the particles exhibited a core region of enhanced electron density. Catalase cytochemistry of peak fractions confirmed the peroxisome identity of the organelles. Peroxisome-enriched subcellular fractions were used to investigate the properties of gastropod D-aspartate oxidase and D-amino acid oxidase activities. The substrate and inhibitor specificities of the two activities demonstrated that two distinct enzymes were present analogous to, but not identical to, the equivalent mammalian peroxisomal enzymes.     

Separate monophenolase and o-diphenolase enzymes in Triticum aestivum

Monophenolase and o-diphenolase activities of polyphenol oxidase are usually thought to be a part of the same enzyme complex. It has now been demonstrated that the two catalytic activities of the polyphenol oxidase of wheat grains are separable and reside in different enzymes. The electrophoretically separated monophenolase enzyme showed specificity only for monophenol (l-tyrosine) after its elution from acrylamide gels. Further, this enzyme is confined to the endosperm tissue and is undetectable in the embryonic region of the seedling.     

The molybdoenzymes xanthine oxidase and aldehyde oxidase contain fast- and slow-DTNB reacting sulphydryl groups

The reactivities with an excess of 5-5-dithiobis (2-nitrobenzoic) acid (DTNB) of sulphydryl residues present in xanthine oxidase and aldehyde oxidase were studied and compared. The results show that two classes of sulphydryl groups with quite different reactivities exist in both enzymes either native or denatured. Some of the available sulphydryl residues thus react instantaneously with the DTNB, whereas the others react very slowly following pseudo-first-order kinetics. The number of sulphydryl residues of each class and the rate constant of slowly reacting groups are, respectively, 1.7 and 0.8 in native xanthine oxidase and 1.6 and 1.7 in native aldehyde oxidase. In denatured enzymes, the number of fast- and slow-reacting sulphydryl residues obtained are, respectively, 13.9 and 7.9 in xanthine oxidase and 5.7 and 5.4 in aldehyde oxidase. Analogously, the rate constant for the slowly reacting groups is similar for the two native enzymes, but in denatured aldehyde oxidase it is double that of denatured xanthine oxidase.     

Activities of Cu-containing proteins in Cu-depleted pea leaves

The effect of Cu deficiency on Cu-containing enzymes and on their activities was studied with two subsequent generations of Cu-deficient pea plants ( Pisum sativum L., cv. Progress) grown in low Cu²⁺ media. Cu deficiency caused growth inhibition and a decrease in photosynthesis as well as in the activities of 3 Cu-containing enzymes: diamine oxidase (EC 1.4.3.6), ascorbate oxidase (EC 1.10.3.3) and superoxide dismutase (EC 1.15.1.1). Determinations of photosynthetic electron-transport rates as well as the concentrations of several redox components showed that the target of Cu deprivation in the photosynthetic apparatus is the synthesis of Cu-containing plastocyanin which is positively correlated to the Cu content of the leaves. Inhibited formation of plastocyanin resulted in low activities of photosynthetic electron transport in photosystem I. Under Cu-deficient conditions, the activities of diamine oxidase and ascorbate oxidase were inhibited by about 50% in the first and 80% in the second generation of pea plants. Enzyme assays showed an inhibition of the activities of both the plastidic and cytoplasmic Cu/Zn-containing superoxide dismutases. An observed simultaneous increase of Mn-superoxide dismutase may be a compensation mechanism to partially maintain the total superoxide-dismutase activity under Cu-deficient conditions. This result indicates that the formation of superoxide-dismutase isoenzymes is interdependent and coordinated.     

Iaa oxidase and polyphenol oxidase activities of peanut peroxidase isozymes

Four anionic isozymes (A₁, A₂, A₄ and A₅) from peanut cells in suspension medium possessed IAA oxidase and polyphenol oxidase activities. The specific activities of each of the enzymes differed among the 4 isozymes. The pH optima established in these assays for peroxidase was acidic, for IAA oxidase neutral and for polyphenol oxidase alkaline. All 4 isozymes had different K_m and V_max for the enzyme activities of peroxidase and polyphenol oxidase. The sigmoid kinetics from the IAA oxidase assays for the isozymes probably indicates an allosteric nature.     

Biochemical, electrophoretic and immunological characterization of peroxisomal enzymes in three soybean organs

Biochemical, electrophoretic and immunological studies were made among peroxisomal enzymes in three organs of soybean [Glycine max (L.) Merr. cv. Centennial] to compare the enzyme distribution and characteristics of specialized peroxisomes in one species. Leaves, nodules and etiolated cotyledons were compared with regard to several enzymes localized solely in their peroxisomes: catalase (EC 1.11.1.6), malate synthase (EC 4.1.3.2), glycolate oxidase (EC 1.1.3.1), and urate oxidase (EC 1.7.3.3). Catalase activity was found in all tissue extracts. Electrophoresis on native polyacrylamide gels indicated that leaf catalase migrated more anodally than nodule or cotyledon catalase as shown by both activity staining and Western blotting. Malate synthase activity and immunologically detectable protein were present only in the cotyledon extracts. Western blots of denaturing (lithium dodecyl sulfate) gels probed with anti-cotton malate synthase antiserum, reveal a single subunit of 63 kDa in both cotton and soybean cotyledons. Glycolic acid oxidase activity was present in all three organs, but ca 20-fold lower (per mg protein) in both nodule and cotyledon extracts compared to leaf extracts. Electrophoresis followed by activity staining on native gels indicated one enzyme form with the same mobility in nodule, cotyledon and leaf preparations. Urate oxidase activity was found in nodule extracts only. Native gel electrophoresis showed a single band of activity. Novel electrophoretic systems had to be developed to resolve the urate oxidase and glycolate oxidase activities; both of these enzymes moved cathodally in the gel system employed while most other proteins moved anodally. This multifaceted study of enzymes located within three specialized types of peroxisomes in a single species has not been undertaken previously, and the results indicate that previous comparisons between the enzyme content of specialized peroxisomes from different organisms are mostly consistent with that for a single species, soybean.     

Changes in IAA,Phenolic Compounds,Peroxidase, IAA Oxidase,and Polyphenol Oxidase in Relation to Flower Formation in Crocus sativus

Changes in levels of IAA, phenolic compounds, peroxidase, polyphenol oxidase, and IAA oxidase activities in the corm and the apical bud of Crocus sativusL. during bud growth and development, with special emphasis on the flowering stage, were studied. In the bud, flower formation was accompanied by enhanced activities of peroxidase, polyphenol oxidase, IAA oxidase, and higher contents of phenolic compounds as well as lower levels of IAA. In the corm, during the flower formation, these enzymes showed an opposite behavior. Moreover, the contents of phenolics and IAA in the corm tissues during flower formation and growth were higher than at the other developmental stages. It may be concluded that the transition of saffron plants to flowering is correlated with peroxidase, polyphenol oxidase, and IAA oxidase. Furthermore, these enzymes might exert their roles in the regulation of flowering through their participation in IAA catabolism. The hypothesis of regulation of bud development by an interaction between phenolics and the enzymes involved in IAA catabolism is discussed.     

Effect of Experimental Diabetes on the Catecholamine Metabolism in Rat Brain

The levels of epinephrine, norepinephrine, and dopamine and the activities of tyrosine hydroxylase and monoamine oxidase were estimated in four regions of rat brain during alloxan-induced hyperglycemia and insulin-induced hypoglycemia. Catecholamine levels were estimated by HPLC, and the insulin levels were quantified by radioimmunoassay. The results demonstrated significant increases in the activities of the metabolizing enzymes and levels of catecholamines during experimental conditions. The levels of catecholamines were highest in the cerebral hemispheres, the region associated with high activities of the metabolizing enzymes. Insulin-induced hypoglycemia caused a decrease in the activities of the metabolizing enzymes followed by their recovery within 2 h.     

Molecular biology of plasma membrane redox enzymes: A survey of current knowledge

Summary Despite a large body of evidence for enzymatic activities and physiological functions of plasma membrane redox function, few of these enzymes have been characterized in terms of molecular biology. Examples for these with at least some molecular data up to complete sequences, membrane topology and binding sites for substrates and coenzymes or prosthetic groups are NADH-ferricyanide reductase of Ehrlich ascites membranes, NADH-coenzyme Q reductase of liver, NADH oxidase ectoenzyme of liver and HeLa (and possibly other) cells, protein disulfide isomerase which is widespread, and relatives thereof, as well as cytochromes P-450 andb ₅₅₈, NADPH oxidase of fat and thyroid cells and fat cell amine oxidase. Ferricyanide reductase and coenzyme O reductase may be identical, but NADH oxidase ectoenzyme is distinct and possibly functions also as a disulfide and a copper reductase. On the other hand, the plasma-membrane-located protein disulfide isomerase (PDI), despite its similar enzymatic activity, is completely different from the ectooxidase. The latter is shed from the membrane into the surrounding medium by proteolysis, whereas PDI is not an integral membrane protein and is secreted intact. Another disulfide reductase has been demonstrated in THP-1 cells, which again is totally different from the former two. It turns out that enzymatic activities are insufficient to describe redox enzymes. Special forms of cytochrome P-450 can be induced to expression at the cell membrane of liver, where they are transported by the cytoskeleton-associated secretory pathway. Why some isoforms are expressed at the surface and some are not is not yet clear. Cytochromeb ₅₅₈, the flavocytochrome of neutrophils, is described in other cells too, but there are different isoforms, which are genetically distinct. A relative has also been identified in duodenal cells, where it functions as a ferric reductase involved in iron absorption. NADPH oxidase of fat cells has very similar properties, but the identity is unproved, whereas thyroid oxidase is a non-heme protein which is calcium-sensitive and does not need assembly of subunits for activation. Finally, fat cell membranes also possess a quinone-containing amine-oxidase which may be involved in signaling of glucose-transport regulation, as it is also found in GLUT4-containing vesicles. However, the physiological connection has yet to be demonstrated.