Acid Phosphatases Associated With Phosphorus Deficiency in Wheat: Partial Purification and Properties

1991 ◽  
Vol 18 (6) ◽  
pp. 615 ◽  
Author(s):  
RE Guthrie ◽  
KD Mclachlan ◽  
DGD Marco
Keyword(s):  
Molecular Weight ◽  
Phosphorus Deficiency ◽  
Size Exclusion ◽  
Partial Purification ◽  
Acid Phosphatases ◽  
Ammonium Sulfate Precipitation ◽  
Con A ◽  
Substrate Utilisation ◽  
Purification And Properties ◽  
Exclusion Chromatography

Procedures for the partial purification of two phosphatase isozymes found in phosphorus deficient wheat plants are given. The method employs ammonium sulfate precipitation and hydroxylapatite, Con A-Sepharose, anion exchange and size exclusion chromatography. Measurements of their Km, Vmax, pI and molecular weight are reported. Evidence is provided that there are empirical differences in substrate utilisation between these phosphatase isozymes associated with phosphorus deficient plants.

scholarly journals Peroxidase from infected fruit of Solanum sp. grown in Nsukka

2019 ◽  
Vol 54 (2) ◽  
pp. 131-138
Author(s):  
Omeje KO ◽  
Eze SOO ◽  
FC Chilaka
Keyword(s):  
Molecular Weight ◽  
Quality Control ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Size Exclusion ◽  
Optimum Temperature ◽  
Ammonium Sulfate Precipitation ◽  
Optimum Ph ◽  
Exclusion Chromatography ◽  
The Ideal

In this study, we characterized the activity of peroxidase a quality control enzyme from the infected fruit of Solanum sp. Peroxidase was purified to homogeneity by ammonium sulfate precipitation, dialysis, ion exchange chromatography and size exclusion chromatography. The molecular weight of the native enzyme was 63000 da. The enzyme was shown to have two iso-enzymes with distinct optimum pH of 4.5 and 7.0 and optimum temperature of 40 and 70⁰C. The purified enzyme had broad substrate specificity with o-dianisidine being the ideal substrate. Na+, Ca2+, Mg2+, Mn2+, Cu2+, Al3+ were shown to be activators of the enzyme, while the peroxidase activity was severely inhibited by Co2+. Bangladesh J. Sci. Ind. Res.54(2), 131-138, 2019

Extraction and Partial Purification of Protease from Bilimbi (Averrhoa bilimbi L.)

2013 ◽  
Vol 10 (2) ◽  
pp. 29
Author(s):  
Normah Ismail ◽  
Nur' Ain Mohamad Kharoe
Keyword(s):  
Molecular Weight ◽  
Protein Content ◽  
Ammonium Sulfate ◽  
Molecular Weight Distribution ◽  
Weight Distribution ◽  
Protease Activity ◽  
Protein Concentration ◽  
Temperature Stability ◽  
Partial Purification ◽  
Ammonium Sulfate Precipitation

Unripe and ripe bilimbi (Averrhoa bilimbi L.) were ground and the extracted juices were partially purified by ammonium sulfate precipitation at the concentrations of 40 and 60% (w/v). The collected proteases were analysed for pH, temperature stability, storage stability, molecular weight distribution, protein concentration and protein content. Protein content of bilimbi fruit was 0.89 g. Protease activity of both the unripe and ripe fruit were optimum at pH 4 and 40°C when the juice were purified at 40 and 60% ammonium sulfate precipitation. A decreased in protease activity was observed during the seven days of storage at 4°C. Molecular weight distribution indicated that the proteases protein bands fall between IO to 220 kDa. Protein bands were observed at 25, 50 and 160 kDa in both the unripe and ripe bilimbi proteases purified with 40% ammonium sulfate, however, the bands were more intense in those from unripe bilimbi. No protein bands were seen in proteases purified with 60% ammonium sulfate. Protein concentration was higher for proteases extracted with 40% ammonium sulfate at both ripening stages. Thus, purification using 40% ammonium sulfate precipitation could be a successful method to partially purify proteases from bilimbi especially from the unripe stage. 

Characterisation of Persistent Anti-Xa Activity Following Administration of the Low Molecular Weight Heparin Enoxaparin Sodium (Clexane)

1994 ◽  
Vol 72 (02) ◽  
pp. 275-280 ◽  
Author(s):  
David Brieger ◽  
Joan Dawes
Keyword(s):  
Molecular Weight ◽  
Enoxaparin Sodium ◽  
Antithrombin Iii ◽  
Anticoagulant Activity ◽  
Active Material ◽  
Biologically Active ◽  
Size Exclusion ◽  
Low Molecular Weight ◽  
Exclusion Chromatography ◽  
Liver And Kidney

SummaryIt is widely reported that persistent anti-Xa activity follows administration of low molecular weight heparins. To identify the effectors of this activity we have injected 125I-labelled Enoxaparin sodium into rabbits and subsequently analysed the circulating radiolabelled material and anti-Xa activity by affinity and size exclusion chromatography. Antithrombin III-binding material derived from the injected drug was responsible for all the anti-Xa amidolytic activity. At early times after injection additional anticoagulant activity which was largely attributable to tissue factor pathway inhibitor was measured by the Heptest clotting assay after removal of glycosaminoglycans from plasma samples. Small radiolabelled fragments, including penta/hexasaccharide with affinity for antithrombin III, were detectable in the circulation 1 week later, and sulphated oligosaccharides persisted for 3-4 weeks. Significant quantities of radiolabel remained in the liver and kidney several weeks post-injection; these organs may sequester some of the injected drug and give rise to circulating biologically active material by degradation and secretion of catabolic products into the plasma.

A study on the kinetics and thermal properties of polystyrene/diatomite nanocomposites prepared via in situ ATRP

2018 ◽  
Vol 33 (2) ◽  
pp. 180-197 ◽  
Author(s):  
Khezrollah Khezri ◽  
Yousef Fazli
Keyword(s):  
Molecular Weight ◽  
In Situ Polymerization ◽  
Structural Characteristics ◽  
Nitrogen Adsorption ◽  
Linear Increase ◽  
Size Exclusion ◽  
Scanning Calorimetry ◽  
Morphological Studies ◽  
Exclusion Chromatography

Pristine mesoporous diatomite was employed to prepare polystyrene/diatomite composites. Diatomite platelets were used for in situ polymerization of styrene by atom transfer radical polymerization to synthesize tailor-made polystyrene nanocomposites. X-Ray fluorescence spectrometer analysis and thermogravimetric analysis (TGA) were employed for evaluating some inherent properties of pristine diatomite platelets. Nitrogen adsorption/desorption isotherm is applied to examine surface area and structural characteristics of the diatomite platelets. Evaluation of pore size distribution and morphological studies were also performed by scanning and transmission electron microscopy. Conversion and molecular weight determinations were carried out using gas and size exclusion chromatography, respectively. Linear increase of ln ( M0/M) with time for all the samples shows that polymerization proceeds in a living manner. Addition of 3 wt% pristine mesoporous diatomite leads to an increase of conversion from 72% to 89%. Molecular weight of polystyrene chains increases from 11,326 g mol−1 to 14134 g mol−1 with the addition of 3 wt% pristine mesoporous diatomite; however, polydispersity index values increases from 1.13 to 1.38. Increasing thermal stability of the nanocomposites is demonstrated by TGA. Differential scanning calorimetry shows an increase in glass transition temperature from 81.9°C to 87.1°C by adding 3 wt% of mesoporous diatomite platelets.

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