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1.
  • 1.1. Activities of the three ammonia-forming enzymes, glutamate dehydrogenase, AMP deaminase and serine dehydrase (SerDH), were measured in tissues of gill, digestive diverticula, mantle and foot muscle of the brackish-water bivalve Corbicula japonica.
  • 2.2. High levels of SerDH activity were detected in gill and digestive diverticula, while the activity levels of the other two enzymes were low.
  • 3.3. The result suggests the significance of SerDH in amino acid degradation of this species.
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2.
  • 1.1. Subcellular location of dihydropyrimidinase and NCβA-amidohydrolase2 was studied in a cell suspension culture of tomato (Lycopersicon esculentum cv. Lukullus) and in Euglena gracilis.
  • 2.2. By differential centrifugation, crude extracts were separated into ten fractions. Activities of both enzymes were found mainly in cytosolic fractions marked by EDH (tomato) and glu-6-P-DH (E. gracilis).
  • 3.3. A cytosolic location was also found by a 20–60% and a 17.5–30% sucrose density gradients.
  • 4.4. Using mitochondrial marker enzymes such as fumarase, SDH, CS and MDH, a mitochondrial occurrence of both enzymes or their release from mitochondria can be excluded by sucrose gradient centrifugations. This can also be achieved using purified mitochondria prepared from tomato cells by two subsequent sucrose gradients.
  • 5.5. A possible vacuolar location of dihydropyrimidinase and NCβA-amidohydrolase was excluded by comparing their activities in isolated protoplasts and purified vacuoles which were characterized by their marker enzyme α-mannosidase.
  • 6.6. A nuclear location of both enzymes and/or their release from the nucleus during procedures used cannot be excluded.
  • 7.7. The results are discussed in relation to subcellular location to other pyrimidine-metabolizing enzymes in plant cells.
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3.
  • 1.1. Activities of nine glycolytic and related enzymes were measured in lantern muscle extracts of the echinoids Arbacia lixula, Echinometra lucunter and Lytechinus variegatus.
  • 2.2. The specific activities of these enzymes were comparatively low, being often the highest in L. variegatus and the lowest in A. lixula. The major differences referred to HK, PGK and G-6-PDH activities.
  • 3.3. Noticeable differences in LDH activities were recorded in comparison with other invertebrate muscles. The implications of these results are discussed.
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4.
  • 1.1. NAD(P)H dehydrogenase from rabbit liver was purified to electrophoretic homogeneity using a procedure also found applicable for the rat liver enzyme.
  • 2.2. Rabbit and rat liver enzymes showed different behaviour in isoelectric focusing and different Km values and turnover numbers.
  • 3.3. Both enzymes were inhibited to similar extents by warfarin.
  • 4.4. The rabbit enzyme is composed of two subunits of mol. wt 27,000 and contained 1 FAD group per subunit.
  • 5.5. Some absorption and circular dichroism properties of the rat enzyme are shown.
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5.
  • 1.1. Chemical structures were determined for the cuticular alkanes, alkenes, and certain of the alkadienes for 11 D. virilis group species.
  • 2.2. Male-specific hydrocarbons occurred in five species: these were 9-heneicosene in D. americana and D. novamexicana, 10-heneicosene in D. virilis, 5,13- and 5,15-pentacosadienes in D. kanekoi, and 9-pentacosene in one strain of D. lummei.
  • 3.3. Hydrocarbon profiles of newly emerged flies always differed from mature files.
  • 4.4. Relationships among the species, with respect to hydrocarbon profiles, were investigated by cluster analysis.
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6.
  • 1.1. The presence of a renin-angiotensin-like system has been investigated in the Antarctic fishes Chionodraco hamatus (Fam. Channichthydae) and Pagothenia (Trematomus) bernacchii (Fam. Notothenidae).
  • 2.2. A renin-like activity is present in plasma and kidney of both the white blooded (Chionodraco) and the red blooded (Pagothenia) species.
  • 3.3. An angiotensin converting enzyme-like activity has been demonstrated in plasma, gills and kidneys of both species. The activity is inhibited by high temperature.
  • 4.4. From our data a renin-angiotensin-like system is present in the Antarctic fishes studied but the cascade of enzymes is active only at low temperatures.
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7.
  • 1.1. Gluconeogenesis from 14C-substrates was measured in liver slices from marine teleosts.
  • 2.2. 0.56 to 2.78 μmols of lactate were incorporated/g wet wt/hr with the higher rates corresponding to the active species.
  • 3.3. Snapper (Chrysophrys auratus) and bream (Acanthopagrus butcheri) exercised continuously for 14 days showed a substantial increase in the incorporation of lactate; snapper confined for 4 months showed a significant decrease in the incorporation of lactate, compared to freshly caught individuals.
  • 4.4. Pyruvate carboxylase and fructose 1,6-diphosphatase were found in red muscle. Some phosphoenolpyruvate carboxykinase may also be present. The three enzymes were present in liver. Possible roles for the enzymes in teleost muscle are discussed.
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8.
A kinetic analysis of the closed bicyclic enzyme cascades is presented.
  • 1.1. It includes the dependence on time from the onset of the reaction, of the concentration of the modified and unmodified enzyme species involved and the time course equations of the modificational fractions of the interconvertible enzymes.
  • 2.2. The transient phase equations obtained allow the definition of new regulatory modification properties.
  • 3.3. The expressions for concentrations of the unmodified and modified forms of the interconvertible enzymes, as well as those of the fractional modifications in the steady state are derived as particular cases of the general equations.
  • 4.4. These steady state expressions coincide with those obtained by other authors.
  • 5.5. The analytical results obtained are discussed in relation to the Escherichia coli glutamine syntethase cascade.
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9.
  • 1.1. The activities of S-adenosylmethionine decarboxylase (EC 4.1.1.50) were measured in cell extracts of mantle, hepatopancreas and foot from Mytilus edulis.
  • 2.2. The apparent molecular weights of the enzymes estimated by gel filtration chromatography were 65,000 ± 10,000.
  • 3.3. The enzymes do not require bivalent cations for catalysis and show optimum pH between 7.0–8.0 in phosphate buffer.
  • 4.4. The hepatopancreas enzyme shows different behavior to the other two enzymes against temperature and its activity is strongly inhibited by NH4+.
  • 5.5. The apparent Kms for S-adenosylmethionine were found to be 300, 200 and 250 μM for the hepatopancreas, mantle and foot enzymes, respectively.
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10.
  • 1.1. The effect of myo-inositol on the ability of three species of nematodes to survive desiccation has been studied.
  • 2.2. Survival rates obtained from worms treated with an inositol bathing medium were compared with survival rates of worms treated with distilled or tapwater media.
  • 3.3. Highest survival rates were found in those nematodes that were placed in an inositol solution prior to desiccation.
  • 4.4. Tapwater facilitated higher revival rates than did distilled water in both D. dipsaci and D. myceliophagous.
  • 5.5. No such differences were found for A. tritici.
  • 6.6. The results are discussed in relation to the possible mechanisms of protection afforded by the different bathing media.
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11.
  • 1.1. Two carboxypeptidase-A type of enzymes and two carboxypeptidase-B type of enzymes effecting hydrolysis of Hipp-l-Phe and Hipp-l-Arg respectively, have been purified from E. superba using gel filtration, affinity chromatography and FPLC-anion exchange chromatography. In addition an aminopeptidase has been partly purified.
  • 2.2. The carboxypeptidases had mol. wts of 27,000 (carboxypeptidase A) and 31,000 (carboxypeptidase B).
  • 3.3. Carboxypeptidase A exhibited a broad pH optimum with a maximum at pH 5.5–6.5, whereas carboxypeptidase B had a more narrow pH-optimum with a maximum at pH 7. The aminopeptidase had an optimum at about pH 8.7.
  • 4.4. The carboxypeptidases were inhibited by the chelating agent 1,10-phenanthroline.
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12.
  • 1.1. The utility of biochemical genetic methods of bird identification was investigated for some common species which create a hazard for commercial aviation in Ireland.
  • 2.2. Sixteen enzyme loci were assayed in eight species, using starch gel electrophoresis; three larids, three corvids and two columbids.
  • 3.3. Genera were distinguishable using all but two loci.
  • 4.4. Differences within genera were small, but all species except for the gulls Larus argentatus and L. marinus, could be identified using one or more loci.
  • 5.5. Arising from the success of the method using fresh specimens, a protocol for the electrophoretic identification of traumatized remains of strikes is suggested.
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13.
  • 1.1. The obligate methanol-utilising bacterium strain 4025 contains cytochromes b and c. Cytochrome a is never present.
  • 2.2. The soluble cytochrome c is similar to that from other methylotrophs in reacting (slowly) with carbon monoxide and it can be separated into two types, differing markedly in their isoelectric points.
  • 3.3. Some of the cytochrome b reacts rapidly with carbon monoxide and is thus the likely cytochrome oxidase (cytochrome o).
  • 4.4. The partially purified, NAD+-independent methanol dehydrogenase is similar to such enzymes from the other methanol-utilising bacteria in respect of its prosthetic group, dependence on ammonia or methylamine for activity and its wide substrate specificity.
  • 5.5. The fluorescence seen in colonies of this organism is probably due to a flavin derivative.
  • 6.6. This study of electron transport components does not shed any light on the unusually high copper requirement shown by this methylotroph.
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14.
  • 1.1. Some aspects of the gas exchange system of a diving lizard, Physignathus lesuewii were studied.
  • 2.2. Breathing patterns were analysed.
  • 3.3. Breathing rate increases logarithmically with temperature and Q10 = 1.8. LogBR = −0.237 + 0.0256 T.
  • 4.4. Gas tensions in lung air and arterial and venous blood were measured. Arterial pH declines with increasing temperature.
  • 5.5. Temperature has a marked effect on oxygen affinity of the blood (ΔH = −10.1 kcal mol). A Bohr effect was also noted.
  • 6.6. CO2 equilibrium curves were drawn.
  • 7.7. The results are considered with a view to anticipating the efficiency of the gas exchange system of this species under conditions of variable temperature and during diving.
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15.
  • 1.1. Morphological similarities and differences for the urticating apparatus of three Lepidoptera were studied using a scanning electron microscope.
  • 2.2. Complementary anatomical studies of the urticant apparatus were undertaken to explain the morphological results.
  • 3.3. Biochemical identity of a thaumetopoein-like protein (an urticating protein) was demonstrated for Thaumatopoea urticating hairs but not for Hylesia moth spicules.
  • 4.4. Urticating mechanisms appear to be different across species of Lepidoptera.
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16.
  • 1.1. The observed level and subcellular distribution of the α-glycerophosphate and malate-aspartate substrate shuttle enzymes in liver and colon were consistent with their proposed roles in reducing equivalent transport.
  • 2.2. Km value determinations of shuttle enzymes were performed.
  • 3.3. Substrate shuttles were reconstructed from isolated liver and colon mitochondria which displayed satisfactory respiratory control and P:O ratios.
  • 4.4. The results obtained suggest that while the malate-aspartate shuttle is the primary means of reducing equivalent transport in the liver, the α-glycerophosphate shuttle predominates in the colon.
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17.
  • 1.1. A highly efficient cellulose digestion could be demonstrated in a primitive insect species, Thermobia domestica (Thysanura:Lepismatidae), by the application of a uniformly 14C-labelled substrate.
  • 2.2. Gut extracts exhibit distinct hydrolytic activities toward different cellulosic substrates (cellobiose, sodium carboxymethylcellulose and microcrystalline cellulose). Therefore, the complete cellular complex must be present.
  • 3.3. Besides cellulases, several other carbohydrates occur in the digestive juice, thus reflecting the omnivorous feeding habits of the insect.
  • 4.4. The crop was found to be the main site of carbohydrate digestiopn, also including cellulolysis.
  • 5.5. It is very likely that the cellulolytic enzymes derive from the gut tissues of the firebrat.
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18.
  • 1.1. Patterns of osmoregulation were studied in three species of Swan river atherinids (Leptatherina presbyteroides, lower estuarine and marine; Craterocephalus mugiloides, mid estuarine; Leptatherina wallacei, upper estuarine) over a wide range of salinities.
  • 2.2. The plasma Na+ concentration was elevated with an increase in salinity.
  • 3.3. Haematocrit and body water content decreased with acclimation to higher salinity.
  • 4.4. All three species of atherinids osmotically regulated over a salinity range greater than that which these fish are reported to occur in.
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19.
  • 1.1. The activity of l-gulonolactone oxidase (EC 1.1.3.8) in livers of 49 species of eutherian mammals varied intraspecifically among individuals; coefficients of variation were 0.2 to 0.4 in many species.
  • 2.2. Differences observed in l-gulonolactone oxidase activity among strains of laboratory rats and domestic rabbits are probably genetically controlled.
  • 3.3. Pronounced sex differences in l-gulonolactone oxidase activity were found in some species, particularly in the genera Peromyscus, Reithrodontomys and Onychomys.
  • 4.4. Mormota monax exhibited seasonal variation in l-gulonolactone oxidase somewhat like that previously observed in Sylvilagus floridanus; no such seasonal variation was found in Sciurus carolinensis.
  • 5.5. Hibernation did not affect l-gulonolactone oxidase activity in Spermophilus tridecemlineatus.
  • 6.6. In four species of rodents, Microtus ochrogaster, Tylomys panamensis, Octodon degus and Sigmodon hispidus, l-gulonolactone oxidase activity was not affected by the level of dietary ascorbate.
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20.
  • 1.1. The hydrolysis of glycol chitin preparations by several β-N-acetylglucosaminidases was monitored colorimetrically with the potassium ferriferrocyanide reagent.
  • 2.2. Glycol chitin samples from crab and insect sources varied considerably in chemical composition and susceptibility to enzymatic hydrolysis.
  • 3.3. Insect endochitinase preferred crab glycol chitin as substrate while hen's egg white lysozyme preferred commercial glycol chitin.
  • 4.4. Insect glycol chitin was well hydrolyzed by both enzymes.
  • 5.5. Insect exochitinase did not digest glycol chitin.
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