STUDIES ON PLASMINOGEN: I. FURTHER PURIFICATION OF BOVINE PLASMINOGEN

1961 ◽  
Vol 39 (9) ◽  
pp. 1419-1431 ◽  
Author(s):  
Edmond R. Cole ◽  
Edwin T. Mertz
Keyword(s):  
Sodium Chloride ◽  
Free Boundary ◽  
Bovine Serum ◽  
Potassium Phosphate ◽  
Glycerol Solution ◽  
Isoelectric Precipitation ◽  
Diethylaminoethyl Cellulose ◽  
Maximum Activation ◽  
Time Required ◽  
Column Product

Crude bovine plasminogen, prepared from bovine serum by 30% saturation with ammonium sulphate, was partially purified by isoelectric precipitation at pH 5.3, then purified by chromatography on columns of diethylaminoethyl-cellulose. Additional purification of the column product was obtained by precipitation of plasminogen from solution with potassium phosphate. The most highly purified bovine plasminogen preparation, assaying 187 esterase units per mg nitrogen, represents a 28-fold purification of crude plasminogen. The over-all recovery from crude plasminogen was 15–20%. Sodium chloride inhibited crude plasminogen but had no effect on the activation of the most highly purified bovine plasminogen preparations. Bovine plasminogen could be spontaneously activated in 50% glycerol solution, but the degree of activation and the time required for maximum activation was also dependent on the purity of the preparation. Free boundary electrophoresis of purified preparations indicated that bovine plasminogen is associated with the major, faster-migrating component.

THE SOLUBLE PROTEINS OF THE MUSCLE TISSUE OF THE HADDOCK

1931 ◽  
Vol 6 (1) ◽  
pp. 1-11 ◽  
Author(s):  
J. F. LOGAN
Keyword(s):  
Sodium Chloride ◽  
Aqueous Solutions ◽  
Muscle Tissue ◽  
Soluble Protein ◽  
Potassium Phosphate ◽  
Extraction Methods ◽  
Water Soluble ◽  
Tabular Form ◽  
Water Soluble Protein ◽  
Isoelectric Points

As a contribution to the chemistry of muscle tissue, the solubility of the protein of haddock muscle in aqueous solutions of sodium chloride and neutral potassium phosphate, respectively, was determined. The results are expressed in tabular form and graphically in the form of solubility curves. A water-soluble protein and also a salt-soluble protein were isolated from dialyzed haddock muscle by extraction methods. These proteins were obtained in a comparatively pure condition by precipitation from solution in the region of their isoelectric points.

Attachment of the flagellate Giardia lamblia: role of reducing agents, serum, temperature, and ionic composition

1982 ◽  
Vol 2 (4) ◽  
pp. 369-377
Author(s):  
F D Gillin ◽  
D S Reiner
Keyword(s):  
Sodium Chloride ◽  
Ionic Strength ◽  
Oxygen Tension ◽  
Giardia Lamblia ◽  
Bovine Serum ◽  
Ionic Composition ◽  
Short Term ◽  
Reduced Temperature

The flagellated protozoan Giardia lamblia has been grown only in highly complex media under reduced oxygen tension. Therefore, the organic and physiological requirements for in vitro attachment and short-term (12-h) survival of this organism were determined. In defined maintenance media, a thiol reducing agent (e.g., cysteine) was absolutely required for attachment and survival of this aerotolerant anaerobe. The crude bovine serum Cohn III fraction greatly stimulated attachment and survival. Attachment was decreased at a reduced temperature (24 degrees C as compared with 35.5 degrees C) and absent at 12 degrees C or below. Attachment and survival were strongly dependent upon pH and ionic strength, with optima at pH 6.85 to 7.0 and 200 to 300 mosmol/kg. Sodium chloride was better tolerated than KC1. Reduction of Ca2+ and Mg2+ to below 10(-8) M did not significantly affect attachment.

On the control of crystal growth in bovine serum albumin-sodium chloride thin film gels

1999 ◽  
Vol 2 (1) ◽  
pp. 79-89 ◽  
Author(s):  
Céline Annarelli ◽  
Laurence Reyes ◽  
Jean Fornazero ◽  
Jacques Bert ◽  
Richard Cohen ◽  
...  
Keyword(s):  
Thin Film ◽  
Crystal Growth ◽  
Sodium Chloride ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

scholarly journals Low–Temperature Storage and the Viability Preservation of Streptomyces

2019 ◽  
Vol 48 (3) ◽  
pp. 34-40
Author(s):  
Татьяна Выборнова ◽  
Tatyana Vybornova ◽  
Наталья Шарова ◽  
Natalya Sharova ◽  
Анастасия Принцева ◽  
...  
Keyword(s):  
Sodium Chloride ◽  
Low Temperature ◽  
Corn Starch ◽  
Activity Level ◽  
Glycerol Solution ◽  
Inhibitor Activity ◽  
Biosynthetic Activity ◽  
Initial Inoculum ◽  
Low Temperature Storage ◽  
Temperature Storage

The most effective way to store microorganisms of different taxonomic groups is at low temperatures from minus 12°C to minus 150°C. The present research features the influence of low temperature (minus 12°C and 18°C) on the viability of collection strains of actinomycetes Streptomyces lucensis VKPM Ac-1743 and Streptomyces violaceus VKPM Ac-1734, producers of glycosidase inhibitors. The strains were stored without a cryoprotector in a 15% glycerol solution and 0.9% sodium chloride aqueous liquid. The research objective was to check their ability to keep their inhibitor activity against pancreatic amylase during corn starch hydrolysate fermentation. The experiment made it possible to determine the titer (CFU in 1 cm3 of the initial inoculum) and inhibitory activity against pancreatic α-amylase. It was revealed that Streptomyces lucensis and Streptomyces violaceus strains in cell initial concentrations of 107 and 108 CFU/cm3 maintained high viability level during four months conservation in 15% glycerol solution and 0.9% sodium chloride aqueous solution at the temperatures of minus 12 °C and minus 18 °C. Most cells survived at the conservation in a 15% glycerol solution at minus 18 °C. The inhibitor activity level in cultural liquid was higher in Streptomyces lucensis and Streptomyces violaceus strains kept in 15% glycerol solution at low the temperatures than in those kept in a 0.9% sodium chloride solution. The cultures kept in a 15% glycerol solution at minus 18 °C had higher inhibitor activity indicators 2600 ± 200 IU/cm3 . The research proved that low-temperature storage of Streptomyces produces no negative effect on the viability and biosynthetic activity of the cultures.

STUDIES ON THE PURIFICATION OF BOVINE PLASMINOGEN (PROFIBRINOLYSIN)

1960 ◽  
Vol 38 (1) ◽  
pp. 1029-1034 ◽  
Author(s):  
Arthur Dalby ◽  
Edmond R. Cole ◽  
Edwin T. Mertz
Keyword(s):  
Calcium Phosphate ◽  
Ammonium Sulphate ◽  
Bovine Serum ◽  
Specific Activity ◽  
Gel Chromatography ◽  
Isoelectric Precipitation ◽  
Ammonium Sulphate Precipitation ◽  
Ph Range

A crude bovine plasminogen product obtained from bovine serum by 30% ammonium sulphate precipitation has been purified 20-fold by means of isoelectric precipitation and calcium phosphate gel chromatography. A threefold purification was achieved by isoelectric precipitation. Plasminogen was precipitated in greatest yield and highest specific activity at 40-fold dilution in the pH range of 5.25–5.50. The conditions under which plasminogen is eluted from calcium phosphate gel columns have been investigated. Plasminogen fractions possessing specific activity seven times that of the isoelectric-precipitated materials have been obtained by elution with phosphate buffers over the range of 0.05 to 0.1 M, pH 6.8.

Non-Machinery-Based System for Cell-Free, Concentrated Autogenous Ascitic Fluid Reinfusion

1995 ◽  
Vol 18 (7) ◽  
pp. 399-406 ◽  
Author(s):  
S. Katoh ◽  
T. Kojima ◽  
S. Morimoto ◽  
K. Inoue ◽  
K. Ida ◽  
...  
Keyword(s):  
Ascitic Fluid ◽  
Clinical Studies ◽  
Bovine Serum ◽  
Protein Concentration ◽  
Treatment Time ◽  
High Protein ◽  
Protein Recovery ◽  
Recovery Ratio ◽  
Time Required

A non-machinery-based system for the reinfusion of ascitic fluid was developed and assessed. In fundamental studies utilizing bovine serum, this procedure proved economical, quick and useful. The most suitable filter was PS-R (#405-2). Bovine serum with a protein concentration below 3.0 g/dl was treated using this system. Samples containing blood (prepared to 0.5% hematocrit) were also treated, but the treatment time required was double that of serum with the same protein concentration. In both cases the protein recovery ratios were about 90%. We conducted clinical studies on 62 occasions (machinery-based system; 31 times, non-machinery-based system; 31 times) on 19 cases of ascites refractory to treatment with various drugs including diuretics. Clarification of the differences between the non-machinery and the machinery-based system, indicated the former to be superior. This new procedure is easier because of its use of no machinery, and the high protein recovery ratio proved its usefulness.

Sporicidal Activity of Chemical Germicides on Bacillus subtilis Spores Under Various Conditions

1994 ◽  
Vol 77 (1) ◽  
pp. 53-57 ◽  
Author(s):  
James W Danielson ◽  
James T Peeler ◽  
Gordon S Oxborrow
Keyword(s):  
Bacillus Subtilis ◽  
Chlorine Dioxide ◽  
Peracetic Acid ◽  
Bovine Serum ◽  
Hard Water ◽  
Soft Water ◽  
Initial Concentration ◽  
Log Reduction ◽  
Time Required ◽  
Intended Use

Abstract Sporicidal tests were conducted on chemical germicides used for reprocessing hemodialyzers. The germicides that were tested for sporicidal activity contain some of the same active ingredients as many other commercial germicides, although instructions for dilution and exposure time may vary according to intended use. Cidex-Dialyzer™ (glu-taraldehyde), formaldehyde, Renalin™ (peracetic acid), and RenNew-D™ (chlorine dioxide) were each tested under the following conditions: at 50, 100, and 150% of the recommended concentration in soft water at 22°C; and at 1× the recommended concentration in soft water at 26.7°C, in hard water at 22°C, and in hard water containing 5% bovine serum at 22°C. Sporicidin-HD™ (glutaraldehyde–phenol) was tested only at the recommended concentration in soft water at 22°C. The time required for a 2-log reduction in the initial concentration of spores ranged from 1.8 min for Renalin at 150% of the recommended concentration to 26.4 h for formaldehyde in hard water containing 5% bovine serum. Cidex-Dialyzer at 50% of the recommended concentration and Sporicidin-HD at the recommended concentration were ineffective against Bacillus subtilis var. niger spores. The sporicidal activities of RenNew-D and formaldehyde were greatly reduced when bovine serum was added to hard water. Renalin had the highest sporicidal activity and was the least affected by each of the conditions tested.

scholarly journals Formation of Nanocomplexes between Carboxymethyl Inulin and Bovine Serum Albumin via pH-Induced Electrostatic Interaction

Molecules ◽  
2019 ◽  
Vol 24 (17) ◽  
pp. 3056 ◽  
Author(s):  
Guiying Huang ◽  
Jun Liu ◽  
Weiping Jin ◽  
Zihao Wei ◽  
Chi-Tang Ho ◽  
...  
Keyword(s):  
Sodium Chloride ◽  
Bovine Serum Albumin ◽  
Complex Formation ◽  
Serum Albumin ◽  
Electrostatic Interaction ◽  
Bovine Serum ◽  
Titration Calorimetry ◽  
Food Ingredients ◽  
Enthalpy Changes ◽  
Ft Ir

As a functional polysaccharide, inulin was carboxymethylated and it formed nanocomplexes with bovine serum albumin (BSA). The success of obtaining carboxymethyl inulin (CMI) was confirmed by a combination of Fourier transform Infrared (FT-IR), Raman spectroscopy, gel permeation chromatography (GPC), and titration. The effects of pH and ionic strength on the formation of CMI/BSA nanocomplexes were investigated. Our results showed that the formation of complex coacervate (pHφ1) and dissolution of CMI/BSA insoluble complexes (pHφ2) appeared in pH near 4.85 and 2.00 respectively. FT-IR and Raman data confirmed the existence of electrostatic interaction and hydrogen bonding between CMI and BSA. The isothermal titration calorimetry (ITC) results suggested that the process of complex formation was spontaneous and exothermic. The complexation was dominated by enthalpy changes (∆Η < 0, ∆S < 0) at pH 4.00, while it was contributed by enthalpic and entropic changes (∆Η < 0, ∆S > 0) at pH 2.60. Irregularly shaped insoluble complexes and globular soluble nanocomplexes (about 150 nm) were observed in CMI/BSA complexes at pH 4.00 and 2.60 while using optical microscopy and atomic force microscopy, respectively. The sodium chloride suppression effect on CMI/BSA complexes was confirmed by the decrease of incipient pH for soluble complex formation (or pHc) and pHφ1 under different sodium chloride concentrations. This research presents a new functional system with the potential for delivering bioactive food ingredients.

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