Decrease of hepatic catalase level by treatment with diallyl sulfide and garlic homogenates in rats and mice

Diallyl sulfide (DAS) is a flavor compound derived from garlic and is active in the inhibition of chemically induced cytotoxicity and carcinogenicity in animal models. This study was conducted to examine the effects of the treatment of DAS and garlic homogenates on the activities of catalase, glutathione peroxidase, and superoxide dismutase. Male Sprague-Dawley rats were treated with DAS i.g. at daily doses of 50 or 200 mg/kg for 8 days, causing the hepatic catalase activity to decrease by 55 and 95%, respectively. Such a decrease in hepatic catalase activity was also observed when the DAS treatment was extended to 29 days. Western blot analysis showed that the DAS treatments resulted in corresponding decreases in the liver catalase protein level. No significant change in the catalase activity in the kidney, lung, and brain was observed with the treatments, but a slight decrease in heart catalase activity was observed. These treatments did not cause significant changes in superoxide dismutase and glutathione peroxidase activities in these tissues. Treatment with DAS at a daily dose of 200 mg/kg for 1-7 days resulted in a gradual decrease in the liver catalase activity to 5% of the control level, but it did not decrease the erythrocyte catalase activity. Treatment of rats with fresh garlic homogenates (2 or 4 g/kg, i.g., daily for 7 days) caused a 35% decrease in liver catalase activity. A/J mice treated with DAS and garlic homogenates also showed a decrease in the liver catalase activity. Diallyl sulfone (DASO2), a DAS metabolite, however, did not effectively decrease catalase activity in mice. The catalase activity was not inhibited by either DAS or DASO2 in vitro. The present results demonstrate that treatment with DAS and garlic homogenates decrease the hepatic catalase level in rats and mice.     

Factors affecting catalase expression in Pseudomonas aeruginosa biofilms and planktonic cells

Previous work with Pseudomonas aeruginosa showed that catalase activity in biofilms was significantly reduced relative to that in planktonic cells. To better understand biofilm physiology, we examined possible explanations for the differential expression of catalase in cells cultured in these two different conditions. For maximal catalase activity, biofilm cells required significantly more iron (25 microM as FeCl(3)) in the medium, whereas planktonic cultures required no addition of iron. However, iron-stimulated catalase activity in biofilms was still only about one-third that in planktonic cells. Oxygen effects on catalase activity were also investigated. Nitrate-respiring planktonic cultures produced approximately twice as much catalase activity as aerobic cultures grown in the presence of nitrate; the nitrate stimulation effect could also be demonstrated in biofilms. Cultures fermenting arginine had reduced catalase levels; however, catalase repression was also observed in aerobic cultures grown in the presence of arginine. It was concluded that iron availability, but not oxygen availability, is a major factor affecting catalase expression in biofilms.     

Properties of residual catalase in the erythrocytes of Japanese-type acatalasemia

Summary In Japanese-type acatalasemia erythrocytes, the presence and properties of residual catalase were determined and compared with those of normal erythrocyte catalase. Residual catalase activity was proved by titration, active staining after polyacrylamide gel electrophoresis, and measurement of oxygen evolution. Residual catalase protein, demonstrated by double immunodiffusion, was similar to that of normal catalase. The properties of residual catalase activity were identical with those of normal catalase activity. It occurred as three fractions of equal specific activity by DEAE column chromatography. These observations suggest that Japanese-type acatalasemia contains residual catalase with properties similar to those of normal catalase.     

Quantitative indices of the activity and the electrophoretic characteristics of staphylococcal catalase]

The average levels of activity of intracellular and extracellular catalase were determined. The activity of intracellular catalase was shown to be significantly higher than that of extracellular catalase, the average level of activity of extracellular catalase being higher in S. aureus than in S. epidermidis. In most of the strains one zone of extracellular catalase and two molecular forms of intracellular catalase were revealed by means of polyacrylamide gel electrophoresis.     

小鼠组织中过氧化氢酶的活性与年龄的关系

为观察小鼠组织中过氧化氢酶的活性与年龄的关系,采用高锰酸钾滴定法测定不同年龄(1、4、18月龄)小鼠肝、肾、肺、心、脾、胃、脑组织中过氧化氢酶的活性。结果显示:小鼠过氧化氢酶在不同组织中活性不同,活性高低顺序基本表现为:肝>肾>肺>心、脾、胃>脑;小鼠肺、心、脾、胃、脑各组织中过氧化氢酶的活性在1～4月龄间随年龄增加而增加,在4～18月龄间随年龄增加而降低;小鼠肝、肾组织中过氧化氢酶的活性在1～4月龄间与年龄相关性不显著,在4～18月龄间随年龄增加而降低。结果表明,小鼠肝、肾、肺、心、脾、胃、脑等组织中过氧化氢酶的活性随年龄变化而变化,机体过氧化氢酶活性的降低与机体衰老密切相关。     

Increased erythrocyte catalase activity in patients with hyperthyroidism

Levels of human erythrocyte catalase activity were determined in 38 patients with thyroidal dysfunction. In patients with hyperthyroidism, erythrocyte catalase activities were found to be higher than the levels of normal subjects (P less than 0.001). In hypothyroidism, erythrocyte catalase activities were of the same order as those of normal subjects. Significantly high positive correlation was found between erythrocytes catalase activity and the levels of thyroxine (r = 0.5794, n = 36, P less than 0.001), and slight positive correlation was detected between catalase activity and the levels of triiodothyronine (r = 0.3978, n = 33, P less than 0.05). A decreased erythrocyte catalase activity was observed when erythrocytes lysate was incubated with thyroid hormones. It was suggested that erythrocyte catalase activity had close relationship with thyroid state, however, direct effect of thyroid hormones were not observed on erythrocyte catalase assay system in vitro.     

Evaluation of a catalase inhibitor in the developmental regulation of maize catalase

A protein which has been shown to inhibit catalase in vitro appears to vary inversely with catalase activity in the maize scutellum during early sporophytic development when assayed using a catalase inhibition assay. This result suggested that the inhibitor protein may play a direct role in regulating catalase activity during this time period. Four experimental approaches were used to evaluate this putative regulatory role, including immunological quantitation of individual catalase isozymes during germination using rocket immunoelectrophoresis, perturbation of normal catalase expression with hydrogen peroxide or allylisopropylacetamide (AIA), examination of a mutant line with an altered catalase developmental program, and direct radioimmunoassay of the inhibitor protein during germination. The results of these experiments indicate that the quantitative changes in catalase activity during development are not mainly due to changes in the expression of the catalase inhibitor. Other possible roles of this protein in catalase regulation are discussed.     

Study of the coinduction by fatty acids of catalase A and acyl-CoA oxidase in standard and mutant Saccharomyces cerevisiae strains

Evidence is presented that Saccharomyces cerevisiae can metabolize fatty acids via the inducible peroxisomal beta-oxidation pathway even when these acids are not the sole carbon source. The fatty acids of chain length of C10-C18 induce acyl-CoA oxidase simultaneously with catalase A but have no effect on catalase T and acyl-CoA dehydrogenase. The coinduction of both acyl-CoA oxidase and catalase A is recorded in strains with both active catalase A and T or displaying only catalase A activity. In mutants lacking catalase A, the induction of acyl-CoA oxidase is observed without a concomitant increase in catalase activity. After centrifugation in a linear Ficoll gradient of the particulate fraction from the cells grown on ethanol and oleate the activity of acyl-CoA oxidase cosediments with catalase A. The relationship of catalase A to acyl-CoA oxidase is discussed.     

畜禽粪便堆肥过程中酶活性及微生物数量的变化研究

实验选取鸡粪和猪粪进行好氧堆肥发酵,研究畜禽粪便腐熟过程中酶活性和微生物的变化趋势以及相互联系。结果表明:过氧化氢酶活性和纤维素酶活性在堆肥初期较高,随后迅速降低,最终过氧化氢酶维持在9~12ml/g之间,纤维素酶维持在12.37~15.07mg/(kg·h)之间,而脲酶活性变化趋势为"升高-降低-升高"。细菌数量变化趋势为"低-高-低";放线菌为"高-低";真菌为"高-低-高"。通过相关分析发现,放线菌可能是影响堆肥中过氧化氢酶和纤维素酶的关键因素。鸡粪中放线菌与过氧化氢酶呈极显著正相关;猪粪中放线菌与过氧化氢酶和纤维素酶呈显著正相关;鸡粪+猪粪中放线菌与过氧化氢酶和纤维素酶呈极显著正相关。     

Factors Affecting Catalase Expression in Pseudomonas aeruginosa Biofilms and Planktonic Cells

Previous work with Pseudomonas aeruginosa showed that catalase activity in biofilms was significantly reduced relative to that in planktonic cells. To better understand biofilm physiology, we examined possible explanations for the differential expression of catalase in cells cultured in these two different conditions. For maximal catalase activity, biofilm cells required significantly more iron (25 μM as FeCl₃) in the medium, whereas planktonic cultures required no addition of iron. However, iron-stimulated catalase activity in biofilms was still only about one-third that in planktonic cells. Oxygen effects on catalase activity were also investigated. Nitrate-respiring planktonic cultures produced approximately twice as much catalase activity as aerobic cultures grown in the presence of nitrate; the nitrate stimulation effect could also be demonstrated in biofilms. Cultures fermenting arginine had reduced catalase levels; however, catalase repression was also observed in aerobic cultures grown in the presence of arginine. It was concluded that iron availability, but not oxygen availability, is a major factor affecting catalase expression in biofilms.     

Catalase formation in Rhodotorula mucilaginosa in relation to the effect of glucose and antibiotics

The developmental pattern of the catalase activity in Rhodotorulamucilaginosa, an obligate aerobe, was investigated in relationto its growth. The pattern of catalase activity does not runin a manner comparable with that of a respiratory capacity,because catalase activity takes a continual rise after the middleof the logarithmic growth, while a respiratory pattern runsa constant level during the corresponding growth phase. Additionof antimycin A to cells with a minimum catalase activity doesnot block the increase in the catalase activity. Chloramphenicoldoes not exert any recognizable effect on the catalase formationwhereas cycloheximide does create an intense inhibitory effect,regardless of addition times on the course of growth. Theseresults show that the synthesizing sites of yeast catalase aredifferent from mitochondria. ¹Present address: Department of Biology, Japan Women's University,Tokyo, Japan (Received February 18, 1970; )     

Effect of age, sex, and smoking on serum catalase activity

In selected hospitalized patients (9294) with normal serum catalase activity, 7.58 per cent higher (p less than 0.001) serum catalase activity was detected in males than in females. With age, serum catalase activity decreased (slope-0.0683) in males, increased (slope 0.101) in females and did not change in all patients (slope 0.049). Cigarette smoking did not influence serum catalase activity (p greater than 0.05).     

Catalase Activity of Nodules in the Ureide- and Amide-transporting Legume Plants

The relations of catalase activity to the efficiency of symbiotic dinitrogen fixation and leghemoglobin (Lb) content were investigated in roots and nodules of several legume plant species together with the catalase distribution between the inner bacteroidal and the outer cortical nodule tissues. The catalase activity in the nodules exceeded that of the roots of the amide- and ureide-synthesizing plant species by one and two orders of magnitude. During the growth period, catalase activity and Lb content changed in parallel and reached their highest levels early in the stage of flowering or fruit formation, depending on plant species. In the case of effective symbiosis, catalase activity in the nodules was 2.5–5 times higher than in the case of ineffective symbiosis. Catalase activity in the bacteroidal zone of the nodules was several times higher than that of the cortical tissue, and two nodule tissues differed in catalase activity more notably in the plant species exporting ureides. The authors suggest that high catalase activity in the nodules, especially in their bacteroidal zone, is essential for the efficient functioning of the symbiotic system of dinitrogen fixation in both ureide- and amide-transporting plants.     

The peroxidatic and catalatic activity of catalase in normal and acatalasemic mouse liver

Monomeric, dimeric and tetrameric forms of mouse liver catalase have been shown to express peroxidatic activity while the tetrameric form expresses the catalic activity. Autosomally inherited acatalasemia, produced by X-ray irradiation of mice results in almost complete loss of catalic activity of catalase but has no effect on the peroxidatic activity. Liver catalase from normal and acatalasemic mice was purified by following the catalic and peroxidatic activity, respectively. Antiserum produced in rabbit against catalase from normal mouse completely precipitated the catalatic and peroxidatic activity from normal liver, and peroxidatic activity from the acatalasemic liver homogenate. Similar results were obtained when antiserum against peroxidase from acatalasemic mice was used. These studies indicate that acatalasemia in mice is due to a structural gene mutation which leads to synthesis of structurally altered catalase subunits. The altered subunits express peroxidatic activity but do not combine to form a tetramer which expresses catalatic activity.     

The role of catalase in hydrogen peroxide resistance in fission yeast Schizosaccharomyces pombe.

The role of catalase in hydrogen peroxide resistance in Schizosaccharomyces pombe was investigated. A catalase gene disruptant completely lacking catalase activity is more sensitive to hydrogen peroxide than the parent strain. The mutant does not acquire hydrogen peroxide resistance by osmotic stress, a treatment that induces catalase activity in the wild-type cells. The growth rate of the disruptant is not different from that of the parent strain. Additionally, transformed cells that overexpress the catalase activity are more resistant to hydrogen peroxide than wildtype cells with normal catalase activity. These results indicate that the catalase of S. pombe plays an important role in resistance to high concentrations of hydrogen peroxide but offers little in the way of protection from the hydrogen peroxide generated in small amounts under normal growth conditions.     

Studies on catalase compartmentation in digitonin-treated rat hepatocytes

The cellular compartmentation of catalase was studied in digitonin-permeabilized rat hepatocytes. A biphasic dose-response curve was observed for the unmasking of catalase activity by digitonin in latency studies. About 40-60% of the total catalase activity was seen in the range of 5-200 microM digitonin compared to 13% free activity in control preparations without digitonin. The free catalase activity began to increase again above 300 micron digitonin, and all latency was lost around 500 microM and above. These results indicate that there exists in rat hepatocytes catalase with two levels of crypticity to digitonin, only one of which was seen in a mixed organelle preparation containing peroxisomes.     

Survival of Fungi in Hyperbaric Oxygen in Relation to Changes in Catalase Activity

Survival of replacement cultures of Mucor species in oxygenat 10 atm was markedly affected by the carbon source; culturesreplaced on glucose media survived for a much shorter periodthan cultures on water while 1 per cent ethanol increased thesurvival time. This effect of carbon source on survival wascorrelated with changes in catalase activity; in the presenceof glucose and other carbohydrates, catalase activity decreasedwhereas on 1 per cent ethanol a large increase in catalase activityoccurred which was maintained for several days. An increasein catalase activity also occurred on methanol, pyruvate, glycerol,and formate. Induced changes in peroxidase activity were similarto those shown by catalase but the activity of three other enzymesdecreased in hyperbaric oxygen on all media.     

An examination of the oxidation of mercury vapor by rat brain homogenate

The oxidation of mercury vapor (Hg degrees) to divalent inorganic mercury (Hg2+) was studied in rat brain homogenates. By using a "degassing" method, it was possible to speciate the mercury present in the homogenate and, for the first time, to measure the rate of oxidation as a function of the substrate (Hg degrees) concentration. Mercury oxidation was first-order with respect to substrate concentration at all concentrations tested, and the first-order rate constant for the oxidation process was proportional to homogenate concentration. The role of catalase compound I in mercury vapor oxidation by brain homogenate was examined by observing the effects of two inhibitors of catalase (catalase compound I) on homogenate mercury-oxidizing activity and catalase activity. Sodium azide (50 mM) completely inhibited both mercury-oxidizing activity and catalase activity. Aminotriazole (3-amino-1H-1,2,4-triazole) (50 mM) completely inhibited only mercury-oxidizing activity; some residual catalase activity was found in the aminotriazole-treated homogenate. It was concluded that catalase compound I plays a major role in the oxidation of Hg degrees, but the possibility that catalase-independent pathways make a minor contribution cannot be excluded.     

A study of the catalase monomer produced by lyophilization

Lyophilization of Dounce and Mourtzikos beef liver catalase (Prep. Biochem. 11 (1981) 501-523) under specified conditions produced conformationally altered but not completely denatured catalase monomer which retained both significant catalatic activity and peroxidatic activity towards ethanol. The same lyophilization procedure used with Sigma Co. catalase produced a mixture of conformationally altered catalase monomer and conformationally altered tetramer which showed still higher catalatic and peroxidatic activities; this was attributed to the presence of the altered tetramer. The catalase monomer obtained by the use of Dounce and Mourtzikos catalase is completely reducible by dithionite, as shown by the two-banded spectrum of the reduced material, but apparently retains enough of its native conformation to show some enzymatic activity, since the fully denatured monomer shows no catalatic or peroxidatic activity towards ethanol. The conformationally altered catalase tetramer, which shows more enzymatic activity than the monomer, evidently retains a higher proportion of its native conformation than the monomer, but still appears to be fully reducible with dithionite. Horseradish peroxidase after reduction with dithionite shows spectral bands at positions close to those of reduced lyophilized catalase, but the relative band heights and contours are different. A possible explanation for the observed differences in lyophilization products depending on the starting material (Sigma Co. catalase versus catalase of Dounce and Mourtzikos) is presented.