AN ANTIVIRAL SUBSTANCE FROM PENICILLIUM CYANEO-FULVUM BIOURGE: I. PRODUCTION AND PARTIAL PURIFICATION

1965 ◽  
Vol 11 (6) ◽  
pp. 913-919 ◽  
Author(s):  
Patricia M. Cooke ◽  
J. W. Stevenson
Keyword(s):  
Ammonium Sulfate ◽  
Ethyl Alcohol ◽  
Antiviral Agent ◽  
Partial Purification ◽  
Fractional Precipitation ◽  
Antiviral Substance

Penicillium cyaneo-fulvum Biourge, which produces a toxin-neutralizing substance, has been shown to produce a separate and distinct antiviral agent. The two products may be separated in a semipurified state by fractional precipitation with ammonium sulfate and ethyl alcohol.

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. 

Pengaruh Penambahan Molases Pada Kulit Pisang Kapendis Untuk Media Produksi Xilanase B.Stearothermophillus DSM 22

2019 ◽  
Vol 15 (3) ◽  
Author(s):  
Trismillah
Keyword(s):  
Enzyme Activity ◽  
Ammonium Sulfate ◽  
Banana Peel ◽  
Partial Purification ◽  
Temperature Conditions ◽  
Cavendish Banana ◽  
Working Volume ◽  
Initial Ph ◽  
Xylanase Enzyme

Cavendish banana peel can be used as a substitute for the expensive xylan, while molasses than as a source of carbon as well as nitrogen, minerals and nutrients needed for the growth of microbes that can produce the enzyme. Xylanase produced from Bacillus stearothermopillus DSM 22, using media cavendish banana peels with the addition of molasses 1%, 2%, and 3%. Fermentation is done in a shaker incubator at 550C temperature conditions, initial pH 8, and 250 rpm agitation. The result showed the highest enzyme activity of 4,14 ± 0,16 U/mL min., on the addition 2% molasses after 24 hours. Further fermentation carried out in the fermenter working volume of 3.5 liters, with the condition of temperature 550C, pH 8, aeration 1 vvm, agitation 250 rpm, the highest spesific enzyme of activity of 51,62 ± 0,16 U/mg after 24 hours. Partial purification of xylanase enzyme fermentation is done with the results of microfiltration, ultrafiltration, ammonium sulfate (0-80%) and dialysis. There is an increase in the purity of the enzyme at each stage of purification, the highest purity on dialysis 3.23 times of crude enzymes.Kulit buah pisang kapendis dapat digunakan sebagai pengganti xilan yang harganya mahal, sementara molases selain sebagai sumber karbon serta nitrogen, mineral dan nutrisi dibutuhkan untuk pertumbuhan mikroba yang dapat menghasilkan enzim. Xilanase yang dihasilkan dari Bacillus stearothermopillus DSM 22, menggunakan media kulit pisang kapendis dengan penambahan molase 1%, 2%, dan 3%. Fermentasi dilakukan dalam shaker inkubator pada temperatur 550C, pH awal 8, dan agitasi 250 rpm. Hasilnya menunjukkan aktivitas enzim tertinggi 4,14 ± 0,16 U/mL min., pada penambahan 2% molases setelah 24 jam. Selanjutnya fermentasi dilakukan di dalam fermentor, volume kerja dari 3,5 liter, dengan kondisi temperatur 550C, pH 8, aeration 1 vvm, agitasi 250 rpm, aktivitas spesifik tertinggi 51,62 ± 0,16 U/mg setelah 24 jam. Pemurnian parsial fermentasi enzim xilanase dilakukan dengan hasil mikrofiltrasi, ultrafiltrasi, amonium sulfat (0-80%) dan dialisis. Ada peningkatan kemurnian enzim pada setiap tahap pemurnian, kemurnian tertinggi pada dialisis 3,23 kali dari enzim kasar.Keywords: Xylanase, B. stearothermophillus DSM 22, Cavendish banana peel, molasses, enzyme activity

Isolation of the virus inhibitor from the root extract of Boerhaavia diffusa inducing systemic resistance in plants

1979 ◽  
Vol 57 (11) ◽  
pp. 1214-1217 ◽  
Author(s):  
H. N. Verma ◽  
L. P. Awasthi ◽  
K. C. Saxena
Keyword(s):  
Molecular Weight ◽  
Organic Solvents ◽  
Preliminary Analysis ◽  
Antiviral Agent ◽  
Systemic Resistance ◽  
Partial Purification ◽  
Root Extract ◽  
Virus Inhibitor ◽  
Boerhaavia Diffusa

An antiviral agent, active against spherical and tubular viruses in hypersensitive and systemic hosts, has been isolated from the roots of Boerhaavia diffusa. Partial purification of inhibitor by organic solvents, Sephadex gel, and protein precipitants has been achieved. Preliminary analysis indicates that the inhibitor may be a glycoprotein with a molecular weight of 16 000–20 000 daltons.

scholarly journals Partial purification of thrombopoietin from the plasma of thrombocytopenic rabbits

Blood ◽  
1979 ◽  
Vol 54 (2) ◽  
pp. 377-388 ◽  
Author(s):  
BL Evatt ◽  
J Levin ◽  
KM Algazy
Keyword(s):  
Ammonium Sulfate ◽  
Phosphate Buffer ◽  
Carboxymethyl Cellulose ◽  
Room Temperature ◽  
Deae Cellulose ◽  
Partial Purification ◽  
Elution Volume ◽  
Ammonium Sulfate Saturation ◽  
Citrate Phosphate ◽  
Citrate Phosphate Buffer

Abstract Partially purified thrombopoiesis-stimulating activity was prepared from the plasma of thrombocytopenic rabbits using ammonium sulfate precipitation and DEAE cellulose, Sephadex, and carboxymethyl cellulose chromatography. The protein fraction precipitated by an ammonium sulfate saturation of 60%-80%, previously shown to contain thrombopoiesis-stimulating activity, was used as starting material. Column chromatography was carried out at room temperature at pH 5.6. Under these conditions, thrombopoiesis-stimulating activity (thrombopoietin) was retained by DEAE cellulose (0/03 M citrate- phosphate buffer) and carboxymethyl cellulose (0/003 M citrate- phosphate buffer), and eluted with 0.4 M NaCl. Thrombopoietin was retarded by Sephadex G-100; the ratio of the elution volume to the void volume was 1.32:1. Immunoelectrophoretic analysis of partially purified thrombopoietin indicated that following removal of most of the albumin by DEAE chromatography, only proteins with the mobilities of beta- globulins and albumin and traces of other anodally migrating proteins were detectable in the fractions that contained thrombopoiesis- stimulating activity. Thrombopoietin was not dialyzable and was stable from at least pH 5.6 to 7.5. It was approximately 1000-fold purified following sequential chromatography with DEAE and carboxymethyl cellulose. Although the three fractions described reproducibly stimulated thrombopoiesis, as measured by increased levels of selenomethionine-75Se (75SeM) in the circulating platelets, platelet counts did not increase.

scholarly journals PURIFICATION AND CONCENTRATION OF ENTEROKINASE

1939 ◽  
Vol 22 (4) ◽  
pp. 447-450 ◽  
Author(s):  
M. Kunitz
Keyword(s):  
Ammonium Sulfate ◽  
Fractional Precipitation ◽  
Ph Conditions ◽  
Concentrated Solution

A concentrated solution of purified enterokinase is conveniently prepared from the fluid contents of pigs' duodena by means of fractional precipitation with ammonium sulfate under the proper pH conditions.

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

2013 ◽  
Vol 10 (2) ◽  
pp. 30
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 ofboth 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.

scholarly journals PURIFICATION AND CRYSTALLIZATION OF DIPHTHERIA ANTITOXIN

1942 ◽  
Vol 25 (3) ◽  
pp. 465-485 ◽  
Author(s):  
John H. Northrop
Keyword(s):  
Molecular Weight ◽  
Ammonium Sulfate ◽  
Diphtheria Toxin ◽  
Soluble Fraction ◽  
Thin Plates ◽  
Fractional Precipitation ◽  
Protein Nitrogen ◽  
Sedimentation Constant ◽  
Diphtheria Antitoxin ◽  
Pure Protein

Purified preparations of diphtheria antitoxin have been obtained by digestion of the toxin-antitoxin complex with trypsin, followed by fractional precipitation with ammonium sulfate. The various fractions obtained in this way are all 90 per cent or more precipitated by diphtheria toxin but combine with different quantities of the toxin. The fraction precipitated between 0.33 and 0.5 saturated ammonium sulfate is homogeneous by electrophoresis and ultracentrifuge but does not have constant solubility. A small amount of a more soluble fraction has been obtained which does have constant solubility and satisfies the criteria of a pure protein. This protein crystallizes readily in poorly formed thin plates. It is very unstable and reverts to a less soluble non-crystallizable form. It has a sedimentation constant of 5.7 x 10–13 and a molecular weight of 90,500. It has an antitoxic value of 700–900 flocculation units per mg. protein nitrogen and has an antitoxic value by the protection test of about 700 units per mg. protein nitrogen. The precipitation range of the purified antitoxin with purified toxin is much wider than that with crude preparations.

The use of Sephadex for the electrophoretic resolution and partial purification of β-hydroxybutyric and isocitric dehydrogenases of Azotobacter vinelandii

1969 ◽  
Vol 15 (4) ◽  
pp. 321-325 ◽  
Author(s):  
Peter Jurtshuk ◽  
C. R. Barrera ◽  
S. Manning
Keyword(s):  
Ammonium Sulfate ◽  
Azotobacter Vinelandii ◽  
Partial Purification ◽  
Marker Enzymes ◽  
Electrophoretic Method ◽  
Enzyme Preparations ◽  
Highly Active ◽  
Combined Use ◽  
Soluble Enzymes ◽  
Electrophoretic Resolution

A relatively quick and convenient electrophoretic method, capable of separating and partially purifying soluble enzymes from cell-free extracts, is described. The method presented has the feature of analytical applicability and is ideally used with preparatory amounts of material. This zonal technique was developed with the Svensson-Porath preparatory electrophoresis column by using Sephadex G-25 as the anticonvectant. The D(−)β-hydroxybutyric and isocitric dehydrogenases of Azotobacter vinelandii strain O were used as the marker enzymes, and both were resolved as sharply defined peaks. The combined use of ammonium sulfate fractionation and electrophoresis yielded highly active and partially purified enzyme preparations of the β-hydroxybutyric and isocitric dehydrogenases.

scholarly journals CRYSTALLIZATION OF SALT-FREE CHYMOTRYPSINOGEN AND CHYMOTRYPSIN FROM SOLUTION IN DILUTE ETHYL ALCOHOL

1948 ◽  
Vol 32 (2) ◽  
pp. 265-269 ◽  
Author(s):  
M. Kunitz
Keyword(s):  
Ammonium Sulfate ◽  
Ethyl Alcohol ◽  
Sulfate Solution ◽  
Enzymatic Properties ◽  
Ammonium Sulfate Solution ◽  
Dilute Solutions

Chymotrypsinogen and chymotrypsin crystallize readily from dilute solutions of ethyl alcohol in the absence of salts. The crystals formed in the presence of alcohol differ in appearance from those formed in the presence of ammonium sulfate. Chymotrypsinogen yields well formed polyhedrons instead of fine needles usually produced in ammonium sulfate solution. Chymotrypsin yields fine needles in the presence of alcohol and rhombohedrons in the presence of ammonium sulfate. The enzymatic properties of the crystals formed in the presence of alcohol are identical with those of the crystals isolated in the presence of ammonium sulfate.

Effect of ammonium sulfate fractional precipitation on gel strength and characteristics of gelatin from bighead carp (Hypophthalmichthys nobilis) scale

2014 ◽  
Vol 36 ◽  
pp. 173-180 ◽  
Author(s):  
Xiao-Mei Sha ◽  
Zong-Cai Tu ◽  
Wei Liu ◽  
Hui Wang ◽  
Yan Shi ◽  
...  
Keyword(s):  
Ammonium Sulfate ◽  
Gel Strength ◽  
Bighead Carp ◽  
Fractional Precipitation ◽  
Hypophthalmichthys Nobilis
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