The Influence of Short Ether Anesthesia on Some Liver Enzyme Activities in the Rat

1973 ◽  
Vol 51 (8) ◽  
pp. 604-607 ◽  
Author(s):  
E. Katona
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Malate Dehydrogenase ◽  
Enzyme Activities ◽  
Urate Oxidase ◽  
Arylsulfatase A ◽  
Ether Anesthesia ◽  
Arylsulfatase B ◽  
Thiamine Pyrophosphatase ◽  
Liver Homogenates

Rats were anesthetized by ether inhalation for 4–5 min and sacrificed 1–48 h after anesthesia. From their liver homogenates, the activities of nine enzymes were determined. Activities of urate oxidase and arylsulfatase-A did not change significantly but arylsulfatase-B was slightly decreased. Malate dehydrogenase, arylsulfatase-B, and thiamine pyrophosphatase reached their highest and "malic enzymes" their lowest activities at the same time, 5 h after anesthesia. Alkaline phosphatase first decreased, later increased. Acid phosphatase and glucose-6-phosphatase activities decreased following ether anesthesia. Thesechanges in the enzyme activities generally agree and partly explain previously reported effects of ether anesthesia observed in the serum.

Early Effects of Aminonucleoside on Enzymes in the Golgi Apparatus of Rat Liver

1975 ◽  
Vol 53 (4) ◽  
pp. 549-554 ◽  
Author(s):  
E. Katona ◽  
M. A. Moscarello
Keyword(s):  
Alkaline Phosphatase ◽  
Golgi Apparatus ◽  
Rat Liver ◽  
Intravenous Dose ◽  
Arylsulfatase A ◽  
Single Intravenous Dose ◽  
Renal Lesions ◽  
Arylsulfatase B ◽  
Thiamine Pyrophosphatase ◽  
Early Effects

Rats were injected with a single intravenous dose of aminonucleoside (AMN) and sacrificed 1–48 h later. The activity of several enzymes was assayed in the Golgi apparatus isolated from the liver. Galactosyltransferase activity showed little changes after the AMN, but both acid (EC 3.1.3.2) and alkaline phosphatase (EC 3.1.3.1) activities increased within the first hour and reached control levels only 5–24 h later. Thiamine pyrophosphatase and arylsulfatase A (EC 3.1.6.1) activities also increased and stayed at higher levels for the duration of the experiment. Arylsulfatase B (EC 3.1.6.1) activity decreased shortly after the AMN but later increased to above control levels. These findings support earlier results in which liver ultrastructural and biochemical changes were observed early before renal lesions and proteinuria.

Localization of Enzymes in Certain Secretory Cells of Helix Tentacles

1964 ◽  
Vol s3-105 (69) ◽  
pp. 49-60
Author(s):  
NANCY J. LANE
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Cell Types ◽  
Secretory Cells ◽  
Oval Cells ◽  
Cytoplasmic Localization ◽  
Cell Organelles ◽  
Distinct Cell ◽  
Thiamine Pyrophosphatase ◽  
Ultrastructural Appearance

Secretory cells in the optic tentacles of the snails, Helix aspersa and H. pomatia, have been investigated for the cytoplasmic localization of certain enzymes. The collar cells, considered to be neurosecretory, and the lateral oval cells, were those examined. Acid phosphatase activity is found in the cytoplasm of both cells, in scattered spheroids called the β-bodies. This enzymatic activity indicates that the β-bodies may be lysosomes, as does their ultrastructural appearance. In the 2 cell types, the activity of both alkaline phosphatase and thiamine pyrophosphatase is localized in crescentic bodies considered to correspond to the Golgi lamellae, and in some of the β-bodies. The latter enzyme also exists in the cortices of the α-bodies which, like the β-bodies, are lipid-containing globules. The activity of both cytochrome oxidase and succinate dehydrogenase is found, not only in granules, rods, and filaments interpreted as the mitochondria, but also on the cortices of some or all of the β-bodies. It is concluded that in invertebrates, the lipochondria may be the sites of activity of many different enzymes which in vertebrates are restricted to distinct cell organelles.

scholarly journals Some enzymes present in the walls of mesophyll cells of tobacco leaves

1975 ◽  
Vol 151 (1) ◽  
pp. 141-144 ◽  
Author(s):  
K H Yung ◽  
D H Northcote
Keyword(s):  
Cell Wall ◽  
Acid Phosphatase ◽  
Horseradish Peroxidase ◽  
Malate Dehydrogenase ◽  
Enzyme Activities ◽  
Incubation Medium ◽  
Time Course ◽  
Mesophyll Cells ◽  
Cell Wall Enzymes ◽  
The Difference

Cell-wall enzymes were assayed by the difference between enzyme activities in the whole cell and the protoplast. Both peroxidase (85.2%) and acid phosphatase (21.9%) were located in the wall. However, malate dehydrogenase was found only in the protoplast. A study of the time-course of the release of peroxidase and malate dehydrogenase into the incubation medium from cells either treated with cellulase or untreated, also indicated that peroxidase and not malate dehydrogenase was located in the wall. Only two anodic isoenzymes of peroxidase were present in the cell wall. These were more negatively charged than those of horseradish peroxidase.

Thiamine Pyrophosphatase, Acid Phosphatase, and Alkaline Phosphatase in the Neurones of Helix Aspersa

1963 ◽  
Vol s3-104 (67) ◽  
pp. 401-412
Author(s):  
NANCY J. LANE
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Helix Aspersa ◽  
Size And Shape ◽  
Thiamine Pyrophosphatase ◽  
Sudan Iv

All three phosphatases have been found to be localized mainly in the cortices of bodies which have the distribution, size, and shape of the ‘blue’ and yellow lipid globules. Colouring neurone preparations with the lysochrome Sudan IV, either before or after incubation for thiamine pyrophosphatase or acid phosphatase activity, shows a sudanophil reaction in the medullary spaces surrounded by the cortices that hydrolyse both phosphates. It is concluded that the acid phosphatase and thiamine pyrophosphatase activities, which in vertebrates are present in the lysosomes and Golgi lamellae respectively, are mainly found, in these invertebrate neurones, in the phospholipid lamellae which form the externa of certain of the lipid globules present in the cytoplasm.

scholarly journals Effects of host resistance on the isozymatic patterns of Bipolaris sorokiniana (Dematiaceae, Moniliales)

1997 ◽  
Vol 20 (4) ◽  
pp. 541-546 ◽  
Author(s):  
Marta E. Valim-Labres ◽  
Miguel D.M. Porto ◽  
Aida T.S. Matsumura
Keyword(s):  
Alkaline Phosphatase ◽  
Superoxide Dismutase ◽  
Acid Phosphatase ◽  
Malate Dehydrogenase ◽  
Host Resistance ◽  
Selection Pressure ◽  
Bipolaris Sorokiniana ◽  
Susceptible Cultivar ◽  
Moderately Resistant

Nine isolates of Bipolaris sorokiniana were inoculated on three cultivars of wheat plants (susceptible, moderately resistant, resistant). Eight days after the inoculation, the isolates were recovered (27 isolates) and the following isozymatic patterns were analyzed: esterase, alkaline phosphatase, acid phosphatase, malate dehydrogenase, and superoxide dismutase. The esterase system was the most polymorphic, and the isolates recovered from the susceptible cultivar showed the highest variability. This is evidence that this cultivar exerts low selection pressure on the pathogen

RAT ENDOMETRIUM ENZYMES IN 4-DAY OESTROUS CYCLE AND EARLY PREGNANCY

1977 ◽  
Vol 85 (1) ◽  
pp. 169-176 ◽  
Author(s):  
Jan Jelínek ◽  
Marta Jelínková
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Early Pregnancy ◽  
Enzyme Activities ◽  
Oestrous Cycle ◽  
The Other ◽  
Endogenous Hormones ◽  
Specific Activities ◽  
The Individual

ABSTRACT The specific activities of lactate dehydrogenase (LDH) and its M-type (M-LDH), β-glucuronidase (β-GR), acid phosphatase (ACP) and alkaline phosphatase (AP) were determined. The specific activities of the enzymes (LDH, β-GR) in the myometrium were lower and their changes less pronounced than in the endometrium. We, therefore, determined the enzymes in the rat endometrium only in further experiments. All enzymes react sensitively to the changes induced in the endometrium by endogenous hormones in the course of a 4-day cycle: pro-oestrus (P) is characterized by rather low enzyme activities, oestrus (E) by a peak of LDH and M-LDH and a rise of AP. In metoestrus (M) there is a peak of β-GR, ACP and AP. Dioestrus (D) is characterized by a significant decrease in LDH and M-LDH and by elevated values of all the other enzymes. The values on the individual days of the 4–day cycle were compared with days 4–6 of pregnancy. The reason for this was that if the rats were not mated, they would, respectively, return to pro-oestrus instead of being 4 days pregnant, to oestrus instead of being 5 days pregnant, or to metoestrus instead of being 6 days pregnant. We found the following differences: on day 4 of pregnancy LDH and M-LDH were lower and ACP and AP higher than in P. On day 5 of pregnancy the LDH, M-LDH, β-GR and AP were lower than in E On day 6 of pregnancy the LDH, M-LDH, ACP and especially β-GR, were lower than in M.

scholarly journals CYTOCHEMISTRY OF GOLGI FRACTIONS PREPARED FROM RAT LIVER

1974 ◽  
Vol 60 (1) ◽  
pp. 8-25 ◽  
Author(s):  
Marilyn G. Farquhar ◽  
J. J. M. Bergeron ◽  
George E. Palade
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Acid Phosphatase ◽  
Liver Tissue ◽  
Marker Enzymes ◽  
Reliable Identification ◽  
Fractionation Procedure ◽  
Thiamine Pyrophosphatase ◽  
Opposite Face ◽  
Liver Homogenates

Cytochemical tests for several marker enzymes were applied to liver tissue and to the three Golgi fractions (GF1, GF2, GF3) separated by the procedure of Ehrenreich et al. from liver homogenates of alcohol-treated rats. 5'-Nucleotidase (AMPase) reaction product was found in all three fractions but in different locations: It occurred along the inside of the membrane of VLDL-filled vacuoles in GF1 and GF2, and along the outside of the cisternal membranes in GF3. In the latter it was restricted to the dilated cisternal rims and was absent from the cisternal centers. The AMPase activity found in the fractions by biochemical assay is therefore indigenous to Golgi components and is not due to contamination by plasma membrane. Acid phosphatase (AcPase) reaction product was detected within lysosomal contaminants in GF1 and within many VLDL-filled vacuoles in GF1 and GF2, indicating that AcPase activity is due not only to contaminating lysosomes, but also to enzyme indigenous to Golgi secretory vacuoles. G-6-Pase reaction product was present in GF3 and within contaminating endoplasmic reticulum fragments, but not in other fractions. Thiamine pyrophosphatase (TPPase) was localized to some of the VLDL-filled vacuoles and cisternae in GF1 and GF2, and was not found in the cisternae in GF3. The results demonstrate the usefulness of cytochemical methods in monitoring the fractionation procedure: They have (a) allowed a reliable identification of contaminants, (b) made possible a distinction between indigenous and contaminating activities, and (c) shown, primarily by the results of the TPPase test, that the procedure achieves a meaningful subfractionation of Golgi elements, with GF1 and GF3, representing primarily trans-Golgi elements from the secretory Golgi face, and GF3 consisting largely of cis-Golgi components from the opposite face.

scholarly journals The distributions of some granule-associated enzymes in guinea-pig polymorphonuclear leucocytes

1970 ◽  
Vol 116 (2) ◽  
pp. 207-216 ◽  
Author(s):  
Robert H. Michell ◽  
Morris J. Karnovsky ◽  
Manfred L. Karnovsky
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Guinea Pig ◽  
Soluble Fraction ◽  
Maximum Activity ◽  
Polymorphonuclear Leucocyte ◽  
Urate Oxidase ◽  
Polymorphonuclear Leucocytes ◽  
Granule Fraction ◽  
Two Populations

1. Homogenates of guinea-pig polymorphonuclear leucocytes were separated by differential centrifugation into six particulate fractions and a soluble fraction. 2. The distributions in these fractions of protein, DNA, succinate dehydrogenase, β-glucuronidase, peroxidase, alkaline phosphatase, acid phosphatase (against p-nitrophenyl phosphate and β-glycerophosphate), cathepsin, and catalase were compared. 3. Almost all of the DNA sedimented in the first two pellets, indicating that the nuclei were relatively intact. 4. The four hydrolases and peroxidase showed different distribution patterns, although these activities were previously reported to be localized mainly in the single ‘granule’ fraction isolated from leucocytes. 5. The particles containing peroxidase, acid phosphatase and alkaline phosphatase all exhibited latency. Maximum activity for each enzyme was obtained at roughly similar concentrations of Triton X-100. 6. The acid phosphatase of these cells was distributed between two populations of particles that differed in both sedimentation characteristics and density. The acid phosphatase(s) of the two populations showed slightly different substrate specificities. This bimodal distribution was not an artifact of the procedure used to elicit the cells. 7. Catalase was recovered almost entirely in the soluble fraction and showed no latency in freshly prepared homogenates. No urate oxidase was detected. 8. We conclude that the ‘granule’ fraction of the polymorphonuclear leucocyte, as isolated by previous workers, contains at least three, probably more, populations of particles with different enzyme contents, and that these cells probably do not contain peroxisomes.

scholarly journals Molecular divergence of locally grown pumpkin (Cucurbita maxima) cultivars through some isozyme tests

2012 ◽  
Vol 19 ◽  
pp. 89-93
Author(s):  
ME Haque ◽  
MA Islam ◽  
B Sikdar
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Genetic Polymorphism ◽  
Malate Dehydrogenase ◽  
Polymorphism Analysis ◽  
Cucurbita Maxima ◽  
Extraction Buffer ◽  
Locally Grown ◽  
Its Polymorphism ◽  
Phosphatase Alkaline

Context: Pumpkin (Cucurbita maxima) is highly polymorphic vegetable species and its polymorphism can be analyzed by isozyme molecular marker. Objective: To analyze genetic polymorphism among 10 locally grown pumpkin cultivars by isozyme. Materials and Methods: Fresh leaves of young plant of different cultivars were used for enzyme extraction. Enzyme extracts were prepared by homogenizing of 2 g sample of each cultivar. Prechilled mortar and pestle nestled in ice along with 1% polyvinylpyrrolidone and 2 ml of chilled extraction buffer were used prior to centrifuge. N-PAGE was conducted for different isozymes and stained the gels with specific chemicals for band development. Results: Five isozymes (peroxidase, esterase, acid phosphatase, alkaline phosphatase and malate dehydrogenase) were tested for genetic polymorphism analysis of pumpkin cultivars. Among them esterase, peroxidase and alkaline phosphatase showed polymorphism in different cultivars with 75-, 58.33- and 41.18% respectively. But acid phosphatase and malate dehydrogenase did not show any polymorphism. Esterase and peroxidase produced band quickly than others. Relative mobility of first band of esterase, peroxidase, acid phosphatase, alkaline phosphatase and malate deghdrogenase was 0.063, 0.045, 0.262, 0.07 and 0.093 respectively Conclusion: Out of five isozymes, effective polymorphism was found in esterase and peroxidase test DOI: http://dx.doi.org/10.3329/jbs.v19i0.13006 J. bio-sci. 19 89-93, 2011

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