ENZYMIC CHANGES IN THE CERVIX OF THE RAT AND HAMSTER DURING THE OESTROUS CYCLE AND THE EFFECT OF STEROIDS

1977 ◽  
Vol 72 (2) ◽  
pp. 153-161 ◽  
Author(s):  
ELIZABETH ZACHARIAH ◽  
N. R. MOUDGAL
Keyword(s):  
Alkaline Phosphatase ◽  
Specific Activity ◽  
Protein Biosynthesis ◽  
Hydrolytic Enzymes ◽  
Maximal Activity ◽  
Inhibitory Effect ◽  
Oestrous Cycle ◽  
Single Subcutaneous Injection ◽  
Arylsulphatase A ◽  
Phosphatase Alkaline

SUMMARY Changes in four hydrolytic enzymes, namely acid phosphatase, alkaline phosphatase, arylsulphatase A and B, of the cervix of the rat and hamster have been studied during the 4-day oestrous cycle. All four enzymes showed maximal activity on the day of oestrus and least activity on day 2 of dioestrus. All the enzymes showed significant reduction of activity after ovariectomy, arylsulphatase A and B showing the earliest changes in specific activity. A single subcutaneous injection of 0·02 μg oestradiol-17β/rat increased the specific activity of arylsulphatase A and B from the low ovariectomized level to that observed in control oestrous animals within 18 and 6 h respectively. A higher concentration of oestradiol-17β (2·0 μg) had an inhibitory effect. Progesterone was without effect on arylsulphatase B activity, but when given (2·0 mg) with 0·02 μg oestradiol-17β, it inhibited the response to oestrogen. Cycloheximide prevented the rise in arylsulphatase B activity occurring after oestrogen injection, suggesting a regulation of cervical arylsulphatase B at the level of protein biosynthesis. These results suggest that arylsulphatase B activity may be induced by oestrogen in the cervix of the rat.

scholarly journals Cytochemical localization of certain hydrolytic enzymes at various stages of development of Achlya flagellata mycelium

2015 ◽  
Vol 41 (2) ◽  
pp. 265-282 ◽  
Author(s):  
I. Palczewska ◽  
G. Jagodzka
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Azo Dyes ◽  
Acid Phosphatase Activity ◽  
Hydrolytic Enzymes ◽  
Cytochemical Localization ◽  
Cytoplasmic Granules ◽  
End Products ◽  
E 600 ◽  
Phosphatase Alkaline

The standard coupling azo dyes techniques were used to reveal the activities of acid phosphatase, alkaline phosphatase, esterase and β-galactoidase in the vegetative and reproductive cycle of <i>Achlya flagellata</i>. The end-products of the enzymic reactions, with the exception of E 600 sentisive esterese, which is localized in cytoplasm, occured in cytoplasmic granules. These granules are expected to be spherosomes. Acid phosphatase activity is high in differentiating sporangia, in antheridial hyphae and in degenerating oospheres where hydrolytic processes occur. β-galactosidase is the least active enzyme in the mycelium of <i>Achlya</i>.

scholarly journals Nonhemocyte sources of selected lysosomal enzymes in Biomphalaria glabrata, B. tenagophila and B. straminea (Mollusca: Pulmonata)

1981 ◽  
Vol 76 (3) ◽  
pp. 293-297
Author(s):  
Gary E. Rodrick ◽  
W. Monteiro ◽  
W. A. Sodeman Júnior
Keyword(s):  
Digestive Gland ◽  
Lysosomal Enzymes ◽  
Specific Activity ◽  
Hydrolytic Enzymes ◽  
Biomphalaria Glabrata ◽  
Glutamate Pyruvate Transaminase ◽  
Glutamate Pyruvate ◽  
Specific Activities ◽  
Phosphatase Alkaline ◽  
Glutamate Oxalacetate Transaminase

The specific activities of acid phosphatase, alkaline phosphatase, β-glucuronidase, lysozymes, glutamate-oxalacetate transaminase and glutamate-pyruvate transaminate were determined in the head-foot and digestive gland of Brazilian Biomphalaria glabrata (Touros), B. tenagophila (Caçapava) and B. straminea (Monsenhor Gil). All six enzymes were detected inthe 3000g supernatant. Both cytoplasmic enzymes, glutamate-oxalacetate and glutamate-pyruvate transaminase exhibited the highest specific activities. In the case of the four hydrolytic enzymes assayed, β-glucuronidase exhibited the highest specific activity while lysozyme showed the lowest activity. All six enzymes are thought to be produced by cells within the head-foot and digestive gland of B. glabrata, B. tenagophila and B. straminea.

scholarly journals An Exonuclease I-Aided Turn-Off Fluorescent Strategy for Alkaline Phosphatase Assay Based on Terminal Protection and Copper Nanoparticles

Biosensors ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 139
Author(s):  
Yan Wang ◽  
Ying Yan ◽  
Xinfa Liu ◽  
Changbei Ma
Keyword(s):  
Alkaline Phosphatase ◽  
Human Serum ◽  
Clinical Diagnosis ◽  
Copper Nanoparticles ◽  
Cost Effective ◽  
Fast Method ◽  
Exonuclease I ◽  
Alkaline Phosphatase Assay ◽  
Phosphatase Assay ◽  
Phosphatase Alkaline

As an important DNA 3′-phosphatase, alkaline phosphatase can repair damaged DNA caused by replication and recombination. It is essential to measure the level of alkaline phosphatase to indicate some potential diseases, such as cancer, related to alkaline phosphatase. Here, we designed a simple and fast method to detect alkaline phosphatase quantitively. When alkaline phosphatase is present, the resulting poly T-DNA with a 3′-hydroxyl end was cleaved by exonuclease I, prohibiting the formation of fluorescent copper nanoparticles. However, the fluorescent copper nanoparticles can be monitored with the absence of alkaline phosphatase. Hence, we can detect alkaline phosphatase with this turn-off strategy. The proposed method is able to quantify the concentration of alkaline phosphatase with the LOD of 0.0098 U/L. Furthermore, we utilized this method to measure the effects of inhibitor Na3VO4 on alkaline phosphatase. In addition, it was successfully applied to quantify the level of alkaline phosphatase in human serum. The proposed strategy is sensitive, selective, cost effective, and timesaving, having a great potential to detect alkaline phosphatase quantitatively in clinical diagnosis.

scholarly journals A novel role for WAVE1 in controlling actin network growth rate and architecture

2015 ◽  
Vol 26 (3) ◽  
pp. 495-505 ◽  
Author(s):  
Meredith O. Sweeney ◽  
Agnieszka Collins ◽  
Shae B. Padrick ◽  
Bruce L. Goode
Keyword(s):  
Actin Filament ◽  
Specific Activity ◽  
Inhibitory Effect ◽  
Actin Network ◽  
Inhibitory Effects ◽  
Cellular Functions ◽  
Network Growth ◽  
Assembly Kinetics ◽  
Filament Networks ◽  
First Time

Branched actin filament networks in cells are assembled through the combined activities of Arp2/3 complex and different WASP/WAVE proteins. Here we used TIRF and electron microscopy to directly compare for the first time the assembly kinetics and architectures of actin filament networks produced by Arp2/3 complex and dimerized VCA regions of WAVE1, WAVE2, or N-WASP. WAVE1 produced strikingly different networks from WAVE2 or N-WASP, which comprised unexpectedly short filaments. Further analysis showed that the WAVE1-specific activity stemmed from an inhibitory effect on filament elongation both in the presence and absence of Arp2/3 complex, which was observed even at low stoichiometries of WAVE1 to actin monomers, precluding an effect from monomer sequestration. Using a series of VCA chimeras, we mapped the elongation inhibitory effects of WAVE1 to its WH2 (“V”) domain. Further, mutating a single conserved lysine residue potently disrupted WAVE1's inhibitory effects. Taken together, our results show that WAVE1 has unique activities independent of Arp2/3 complex that can govern both the growth rates and architectures of actin filament networks. Such activities may underlie previously observed differences between the cellular functions of WAVE1 and WAVE2.

scholarly journals Biochemical characterisation of α-glucosidase and β-glucosidase in the alimentary canal of larval Leptinotarsa decemlineata SAY, 1824 (Coleoptera: Chrysomelidae)

2014 ◽  
Vol 83 (4) ◽  
pp. 281-294 ◽  
Author(s):  
Majid Kazzazi ◽  
Fahimeh Dehghanikhah ◽  
Hossein Madadi ◽  
Vahid Hossseininaveh
Keyword(s):  
Incubation Time ◽  
Leptinotarsa Decemlineata ◽  
Digestive Enzymes ◽  
Specific Activity ◽  
Inhibitory Effect ◽  
Maximum Activity ◽  
Pest Population ◽  
Biochemical Characterisation ◽  
Leptinotarsa Decemlineata Say ◽  
Environmentally Safe

ABSTRACT Host plant resistance is an environmentally safe method used for reducing a pest population. Basically, when developing resistant cultivars one needs to study the biochemical characteristics of the digestive enzymes in the insect’s midgut. In this study, the activities of α- and β-glucosidase were determined from Leptinotarsa decemlineata midgut using p-nitrophenyl-α-Dglucopyranoside and p-nitrophenyl-β-D-glucopyranoside as substrates respectively. The results showed that the specific activity of α- and β-glucosidase from 4th instar larvae midguts of L. decemlineata were 5.14 and 5.48 Umg-1 protein respectively. The activity of α-glucosidase was optimal at pH 4, whereas the maximum activity of β-glucosidase in the midgut of L. decemlineata occurred at pH 4-5.5. Both enzymes were stable at pH 3-8 over an incubation time of 8 hours. The respective activities of α- and β-glucosidase were at their highest at 45 °C and 50 °C, but they were not stable at 50 °C during an incubation time of 8 days. Furthermore, our data showed that MgCl2, Tris and urea have a moderate but SDS a severe inhibitory effect on enzyme activity. Biochemical characterisation revealed one and three bands of α- and β-glucosidase activities in the midgut of L. decemlineata respectively.

SIGNIFICANCE OF TRANSAMINASE ACTIVITY OF SERUM

PEDIATRICS ◽  
1959 ◽  
Vol 24 (3) ◽  
pp. 360-361
Author(s):  
SAMUEL P. BESSMAN
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Transaminase Activity ◽  
Specific Approach ◽  
Normal Tissues ◽  
The Past ◽  
Glycolytic Activity ◽  
Enzyme Characteristic ◽  
Phosphatase Alkaline

THE MEASUREMENT of enzyme activity of serum as an indicator of disease has a long history in medicine. In the past, it has been the aim of the designers of these methods to make them as specific as possible for assay of an enzyme characteristic of a particular system or group of similar organs. Examples of these venerable tests are those for amylase, acid phosphatase, alkaline phosphatase and choline esterase in the serum. Warburg made the first departure from this specificity by demonstrating that the activity of triosephosphate dehydrogenase in the serum of animals with cancer was much greater than that of controls. This test was partially specific, for as Warburg had earlier shown, the glycolytic activity of tumors is much greater than that of normal tissues. The non-specific approach became extreme with the introduction of the measurement of the glutamic-oxalacetic transaminase reaction in the diagnosis of acute coronary disease.

Compartmented pyruvate in perfused working heart

1985 ◽  
Vol 249 (3) ◽  
pp. H439-H449 ◽  
Author(s):  
R. Bunger
Keyword(s):  
Specific Activity ◽  
High Specific Activity ◽  
Inhibitory Effect ◽  
Quantitative Agreement ◽  
Myocardial Substrate ◽  
14Co2 Production ◽  
The Mean ◽  
Glycerol 3 Phosphate Dehydrogenase ◽  
Perfused Hearts ◽  
Working Heart

Pyruvate compartmentation and lactate dehydrogenase (LDH) were studied in isolated perfused working guinea pig hearts. The mean intracellular pyruvate (Pyr) contents increased with perfusate Pyr (0-2 mM) but varied only slightly with glucose (0-10 mM) and additional insulin (0.04-5 U/l), respectively. With 5-10 mM glucose plus 5 U/l insulin, but not with Pyr or lactate (Lac) as substrates, a near equilibrium between the LDH and the glycerol-3-phosphate dehydrogenase seemed to exist. Evidence for an inhibitory effect of Pyr on the activity of the LDH system of the perfused hearts was not obtained. With [U-14C]glucose as sole substrate, the specific activity of coronary venous Lac was near half that of precursor glucose. 14CO2 production was thus in quantitative agreement with rates of pyruvate oxidation that were determined as glucose uptake minus (Pyr + Lac) release. In contrast, with 0.2 mM [1-14C]Pyr plus 5 mM glucose, the ratio of 14CO2 production to specific activity of Lac overestimated Pyr oxidation judged from myocardial substrate balances and O2 uptake, respectively; here, at least three pools of [14C]HCO-3 and [14C]lac, respectively, were kinetically demonstrable during washout of trace amounts of 14C-labeled Pyr. Evidently, the specific activity of Lac was equivalent to that of mitochondrial oxidized Pyr provided [14C]glucose was the sole or major precursor of cellular pyruvate. However, exogenously applied [1-14C]Pyr of high specific activity seemed to induce intracellular formation of both a highly and lowly labeled Pyr; the latter Pyr compartment did not seem in ready equilibrium with the cell physiologically prevailing highly labeled Pyr pool.

Acid phosphatase, alkaline phosphatase, and nitrate reductase activity of selected ectomycorrhizal fungi

1989 ◽  
Vol 67 (3) ◽  
pp. 750-753 ◽  
Author(s):  
Iwan Ho
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Nitrate Reductase ◽  
Phosphatase Activity ◽  
Ectomycorrhizal Fungi ◽  
Acid Phosphatase Activity ◽  
Nitrate Reductase Activity ◽  
Reductase Activity ◽  
Phosphatase Alkaline

Seventeen isolates, encompassing five genera and eight species of ectomycorrhizal fungi, were compared for acid phosphatase, alkaline phosphatase, and nitrate reductase activity. Isolates within species differed in enzyme activity and isozyme patterns by host specificity and site (as exemplified by the genus Suillus). Host and site may have affected phosphatase enzyme activity. Generally, the Douglas-fir associates, which dominate in mesic sites, have higher acid phosphatase activity than pine associates, which mostly occupy xeric sites; however, pine associates from mesic sites also have higher acid phosphatase activity (e.g., S. tomentosus). In four isolates of Amanita muscaria, the effect of site was also apparent. Two of them, which have significantly higher acid phosphatase activity than the others, were isolated from mesic sites. The isozyme pattern of the genus Suillus appeared to be separated by host groups. Other isolates with only one species also differed more or less by host groups. They shared at least one band within host groups, except for the two isolates of Paxillus involutus from different hosts. The P. involutus S-403 isolated from an orchard showed much higher nitrate reductase activity than all other isolates. No apparent differences in nitrate reductase activity were found between the other isolates.

Extracellular alkaline phosphatase from marine bacteria: purification and properties of extracellular phosphatase from a marine Pseudomonas sp.

1980 ◽  
Vol 26 (7) ◽  
pp. 833-838 ◽  
Author(s):  
Hiromi Kobori ◽  
Nobuo Taga
Keyword(s):  
Molecular Weight ◽  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Marine Bacteria ◽  
Divalent Cations ◽  
Maximal Activity ◽  
Pseudomonas Sp ◽  
Purification And Properties ◽  
Extracellular Alkaline Phosphatase ◽  
Increased Pressure

Extracellular alkaline phosphatase produced by a marine Pseudomonas was purified to electrophoretic homogeneity. The molecular weight of the enzyme was estimated to be 100 000. The enzyme had maximal activity at pH 11.5. The enzyme was completely inhibited by 1 mM EDTA. However, divalent cations reversed the enzyme inhibition and their order of effectiveness on the reaction was Zn2+ > Ca2+ > Mn2+ > Mg2+ > Sr2+ > Co2+. The enzyme activity was affected by the species of anion whose order of effectiveness was demonstrated to follow the lyotrophic series, Cl− > Br− > NO3−> ClO4− > SCN−. The activity of phosphatase was accelerated linearly by increased pressure until up to 1000 atm (1 atm = 101.325 kPa), and the enzyme activity at 1000 atm was 3.2 times higher than that at 1 atm.

DNA Polymerases of Newborn Rat Brain and Liver

1971 ◽  
Vol 49 (8) ◽  
pp. 978-986 ◽  
Author(s):  
A. D. Bharucha ◽  
M. R. V. Murthy
Keyword(s):  
Rat Brain ◽  
Specific Activity ◽  
Hydrolytic Enzymes ◽  
Polymerase Activity ◽  
Newborn Rat ◽  
Newborn Brain ◽  
Rat Brain And Liver ◽  
Mammalian Tissues ◽  
Optimum Ph ◽  
Sulfhydryl Compounds

DNA polymerase activity was found to be present in appreciable quantities in the extracts of whole tissue (TS) as well as of nuclei (NS) isolated from newborn rat brain and liver. The NS fractions of either of the two tissues exhibited a higher specific activity per unit protein than the corresponding TS fractions. The optimum pH requirements as well as the ability to support DNA synthesis over a long period indicate that the NS fractions were also comparatively less contaminated by interfering substances than the TS fractions.The reaction requirements for the incorporation of TMP residues into DNA by the NS fractions of newborn rat brain and liver and the effect of various inhibitors and hydrolytic enzymes on this reaction were also investigated. These extracts resembled preparations from other mammalian tissues in that they exhibited absolute requirements for the primer DNA, the four complimentary deoxynucleoside triphosphates, and Mg2+ ions. When three of the four deoxynucleoside triphosphates were omitted and only TTP-2-14C was added to the reaction mixture, a limited incorporation of TMP-2-14C into DNA occurred. Other investigations such as the effect of actinomycin and of sulfhydryl compounds revealed that a large part of incorporation by the TS and NS fractions of newborn brain and liver was due to the replicative DNA nucleotidyltransferase enzyme.

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