scholarly journals Nephrotoxicity of aminoglycoside antibiotics :Species difference of rat and mouse in enzymatic activity as an index.

1994 ◽  
Vol 25 (1) ◽  
pp. 243-244
Author(s):  
SHIRO SUZUKI
Keyword(s):  
Enzymatic Activity ◽  
Species Difference ◽  
Aminoglycoside Antibiotics

scholarly journals Influence of Linker Length and Composition on Enzymatic Activity and Ribosomal Binding of Neomycin Dimers

2015 ◽  
Vol 59 (7) ◽  
pp. 3899-3905 ◽  
Author(s):  
Derrick Watkins ◽  
Sunil Kumar ◽  
Keith D. Green ◽  
Dev P. Arya ◽  
Sylvie Garneau-Tsodikova
Keyword(s):  
Enzymatic Activity ◽  
Aminoglycoside Antibiotics ◽  
Substantial Decrease ◽  
Selective Binding ◽  
Linker Length ◽  
Neomycin B ◽  
A Site ◽  
Site Binding

ABSTRACTThe human and bacterial A site rRNA binding as well as the aminoglycoside-modifying enzyme (AME) activity against a series of neomycin B (NEO) dimers is presented. The data indicate that by simple modifications of linker length and composition, substantial differences in rRNA selectivity and AME activity can be obtained. We tested five different AMEs with dimeric NEO dimers that were tethered via triazole, urea, and thiourea linkages. We show that triazole-linked dimers were the worst substrates for most AMEs, with those containing the longer linkers showing the largest decrease in activity. Thiourea-linked dimers that showed a decrease in activity by AMEs also showed increased bacterial A site binding, with one compound (compound 14) even showing substantially reduced human A site binding. The urea-linked dimers showed a substantial decrease in activity by AMEs when a conformationally restrictive phenyl linker was introduced. The information learned herein advances our understanding of the importance of the linker length and composition for the generation of dimeric aminoglycoside antibiotics capable of avoiding the action of AMEs and selective binding to the bacterial rRNA over binding to the human rRNA.

A Method for the Colorimetric Determination of β-Glucuronidase in Urine, Serum, Tissue; Assay of Enzymatic Activity in Health and Disease

1959 ◽  
Vol 36 (2) ◽  
pp. 193-201 ◽  
Author(s):  
Julius A. Goldbarg ◽  
Esteban P. Pineda ◽  
Benjamin M. Banks ◽  
Alexander M. Rutenburg
Keyword(s):  
Enzymatic Activity ◽  
Colorimetric Determination ◽  
Health And Disease ◽  
Urine Serum

Isolation of Antithrombin III from Normal and α1-Antitrypsin-Deficient Human Plasma

1977 ◽  
Vol 38 (02) ◽  
pp. 0475-0485 ◽  
Author(s):  
Anna D. Borsodi ◽  
Ralph A. Bradshaw
Keyword(s):  
Enzymatic Activity ◽  
Isoelectric Focusing ◽  
Antithrombin Iii ◽  
Factor Xa ◽  
Antithrombin Activity ◽  
Bovine Trypsin ◽  
Normal Plasma ◽  
Antitrypsin Deficiency ◽  
Simplified Procedure ◽  
Stimulation Of

SummaryThe plasma of individuals, hetero- or homozygous for α1-antitrypsin deficiency, contains greatly decreased amounts of antithrombin activity as assayed against factor Xa. However, heparin stimulation of the residual antithrombin activity is observed, which is comparable to that of normal plasma. Antithrombins isolated from both normal and α1-antitrypsin deficient plasma by a simplified procedure are indistinguishable in both properties and yields. The microheterogeneity observed on isoelectric focusing of both preparations can be eliminated by treatment with neuraminidase. Neither purified human antithrombin nor α1-antitrypsin, when assayed against bovine trypsin, is stimulated by heparin. These results clearly establish the unique natures of antithrombin and α1-antitrypsin and show that about 75% of the antithrombin activity measured in normal plasma is due to α1-antitrypsin. Estimates of anti thrombin III activity in normal plasma by assays dependent on enzymatic activity can probably be obtained only in the presence of heparin.

Mechanism of Inhibitory Action on Platelet Activation of a Phospholipase A2 Isolated from Lachesis muta (Bushmaster) Snake Venom

1997 ◽  
Vol 78 (05) ◽  
pp. 1372-1380 ◽  
Author(s):  
André L Fuly ◽  
Olga L T Machado ◽  
Elias W Alves ◽  
Célia R Carlinis
Keyword(s):  
Platelet Aggregation ◽  
Enzymatic Activity ◽  
Phospholipase A2 ◽  
Inhibitory Activity ◽  
Thermal Inactivation ◽  
Anticoagulant Activity ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Crude Venom ◽  
Lachesis Muta

SummaryCrude venom from Lachesis muta exhibited procoagulant, proteolytic and phospholipase A2 activities. A phospholipase A2, denoted LM-PLA2 was purified from L. muta venom to homogeneity, through a combination of chromatographic steps involving gel-filtration on Sephacryl S-200 HR and reverse phase chromatography on a C2/C18 column. LM-PLA2 presented a single polypeptide chain with an isoelectric point at pH 4.7 and apparent molecular weight of 17 kDa. Partial aminoacid sequence indicated a high degree of homology for LM-PLA2 with other PLA2 from different sources.LM-PLA2 displayed a potent enzymatic activity as measured by indirect hemolysis of red blood cells but it was neither lethal when injected i.p. into mice nor did it present anticoagulant activity. Furthermore, LM-PLA2 displayed a moderate inhibitory activity on the aggregation of rabbit platelets induced by low levels of ADP, thrombin and arachidonate. In contrast, platelet aggregation induced by high doses of collagen was strongly inhibited by LM-PLA2 as well as ATP-release. Treatment of the protein with p-bromophenacyl bromide or 2-mercapto-ethanol, as well as thermal inactivation studies, suggested that the platelet inhibitory effect of LM-PLA2 is dependent on its enzymatic activity. Thus, the platelet inhibitory activity of LM-PLA2 was shown to be dependent on the hydrolysis of plasma phospholipids and/or lipoproteins, most probably those rich in phosphatidylcholine. Surprisingly, lyso-phosphatidylcholine released by LM-PLA2 from plasma was shown to preferentially inhibited collagen-induced platelet aggregation, in contrast to other PLA2s, whose plasma hydrolytic products indistinctly affect platelet’s response to several agonists.

Degradation of 2,4-dichlorophenol by melamine amine celluloseimmobilized lacasses

TAPPI Journal ◽  
2017 ◽  
Vol 16 (10) ◽  
pp. 559-564 ◽  
Author(s):  
ZHEN WANG ◽  
PINGPING BIN ◽  
YING LIU ◽  
YU LIU ◽  
GUIHUA YANG ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Removal Efficiency ◽  
Immobilized Laccase ◽  
Dialdehyde Cellulose

Epoxidized dialdehyde cellulose (EDC) was prepared and grafted with melamine to obtain melamine grafted epoxidized dialdehyde cellulose (EDC-melamine); the products were characterized by various methods and were used as carriers to immobilize laccase. Results show EDC-melamine can immobilize laccase effectively and have higher enzymatic activity compared with EDC. Furthermore, the enzymatic activity of EDC-melamine was found to be as high as 865 U•mg-1, compared with 140U•mg-1 for EDC. The removal efficiency of 2,4-dichlorophenol (2,4-DCP) for EDC-melamine immobilized laccase was about 71.5% at 40°C for 4 h at 10.0 mg•L-1 and dosage of laccase = 0.2 g/L. The removal efficiency can remain greater than 63%, even after six cycles.

THE EFFECT OF BACTERIAL STRAINS ON THE ENZYMATIC ACTIVITY OF SOILS IN IMPACT ZONE OF ATAMAN LAKE

2020 ◽  
Author(s):  
V.V. Zinchenko ◽  
◽  
E.S Fedorenko ◽  
A.V Gorovtsov ◽  
T.M Minkina ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Dehydrogenase Activity ◽  
Contaminated Soil ◽  
Model Experiment ◽  
Impact Zone ◽  
Bacterial Strains ◽  
The Impact

As a result of the model experiment, an increase in the enzymatic activity of meadow chernozem of the impact zone of Ataman Lake with the introduction of a strains mixture of metal-resistant microorganisms into the soil was established. The experiment has shown that the application of bacterial strains increases the dehydrogenase activity of contaminated soil by 51.8% compared to the variant without remediation

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