scholarly journals PURIFICATION OF THROMBIN

1942 ◽  
Vol 25 (5) ◽  
pp. 679-687 ◽  
Author(s):  
H. Milstone
Keyword(s):  
Ammonium Sulfate ◽  
Specific Activity ◽  
Saturated Ammonium Sulfate ◽  
Sulfate Solutions ◽  
Ionic Calcium

1. Under certain conditions crude prothrombin changes to thrombin without the addition of extraneous activators and in the absence of ionic calcium. 2. Thrombin is soluble in 0.45 saturated ammonium sulfate, whereas crude prothrombin is not. 3. Partially purified thrombin is comparatively stable in concentrated ammonium sulfate solutions at pH 5.2. 4. A method based on the above facts yields a thrombin preparation the specific activity of which is 100 to 175 times the potential specific activity of whole plasma.

A differential protein solubility approach for the depletion of highly abundant proteins in plasma using ammonium sulfate

The Analyst ◽  
2015 ◽  
Vol 140 (24) ◽  
pp. 8109-8117 ◽  
Author(s):  
Ravi Chand Bollineni ◽  
Ingrid J. Guldvik ◽  
Henrik Grönberg ◽  
Fredrik Wiklund ◽  
Ian G. Mills ◽  
...  
Keyword(s):  
Ammonium Sulfate ◽  
Proteomic Analysis ◽  
Protein Solubility ◽  
Plasma Samples ◽  
Differential Protein ◽  
Saturated Ammonium Sulfate ◽  
Sulfate Solutions

This work reports a precipitation and differential protein solubility approach using saturated ammonium sulfate solutions as a depletion and fractionation approach for shotgun proteomic analysis of plasma samples.

Thermodynamic and Transport Properties of Some Disaccharides in Aqueous Ammonium Sulfate Solutions at Various Temperatures

2008 ◽  
Vol 53 (8) ◽  
pp. 1713-1724 ◽  
Author(s):  
Parampaul K. Banipal ◽  
Vickramjeet Singh ◽  
Gurpreet Kaur ◽  
Mandeep Kaur ◽  
Tarlok S. Banipal
Keyword(s):  
Transport Properties ◽  
Ammonium Sulfate ◽  
Sulfate Solutions ◽  
Thermodynamic And Transport Properties

scholarly journals SELECTED PROTEOLYTIC ACTIVITY BY EXTRACTS OF DERMESTID LARVAE

2011 ◽  
Vol 19 (19) ◽  
pp. 79-83
Author(s):  
Lavinel G. IONESCU
Keyword(s):  
Enzyme Activity ◽  
Ammonium Sulfate ◽  
Proteolytic Activity ◽  
Specific Activity ◽  
Proteolytic Enzymes ◽  
High Specific Activity ◽  
Water Extract ◽  
Dermestes Maculatus ◽  
Crude Preparation

The larvae of the Beetle Dermestes maculatus De Geer can subsist on a diet consisting largely of protein. Studies have been undertaken to investigate the nature of proteolytic enzymes. A water extract of the larvae yielded a crude preparation that hydrolyzes gelatin, bide powder, hemoglobin substrate, benzoyl-DL-arginine p-nitroamilide, and glutaryl-L-phenylalanine p-nitroanilide. Enzyme activity was found in a non-dialyzable, heat- and acid0labile portion of the extract yielded two fractions with high specific activity towards gelatin. These are precipitated between 40% to 60% saturation of ammonium sulfate and 60% to 80% saturation. The higher specific activity was observed in the 40%-60% fraction. These results suggest that the larvae of these dermestids contain proteolytic enzymes with actions similar to mammalian trypsin and chymotrypsin. The results also suggest that other proteolytic enzymes may be present as well.

MECHANISMS OF PLATELET AGGREGATION BY ACIDIC MUCOPOLYSACCHARIDE EXTRACTED FROM STICHOPUS JAPONICUS SELENKA IN HUMANS AND RABBITS

1987 ◽  
Author(s):  
J Z Li ◽  
E C-Y Lian
Keyword(s):  
Platelet Aggregation ◽  
Ammonium Sulfate ◽  
Human Platelets ◽  
Platelet Inhibitors ◽  
Rabbit Plasma ◽  
Human Fibrinogen ◽  
Stichopus Japonicus ◽  
Saturated Ammonium Sulfate ◽  
Rabbit Platelets ◽  
Induced Aggregation

It has been reported that acidic mucopolysaccharide extracted from sea cucumber (Stichopus japonicus selenka) (SJAMP) induced the aggregation of human and animal platelets by an unknown mechanism, using platelet-rich plasma (prp) and washed human and rabbit platelets we studied the effects of storage, platelet inhibitors, and various plasmas and their fractions on SJAMP-induced platelet aggregation. we found that the lowest concentrations of SJAMP required for aggregation of human and rabbit platelets were 0.4 and 2 ug/ml respectively. The reactivity of human platelets to SJAMP decreased with time after drawing of blood; rabbit platelets did not show this phenomenon. Platelet inhibitors such as aspirin, indomethacin, apyrase, antimycin, 2-deoxy-D-glucose, and EDTA inhibited by 50 to 100% the aggregation of human platelets induced by SJAMP; but these inhibitors had no effect on SJAMP-induced aggregation of rabbit platelets. Washed human and rabbit platelets were not aggregated by SJAMP. The aggregation of washed human platelets by SJAMP was restored completely by human or rabbit plasma, by human fibrinogen, or by 0 to 30% saturated ammonium sulfate fraction but not by serum. The aggregation of rabbit platelets by SJAMP could only be restored by rabbit plasma or serum, or by 50 to 60% saturated ammonium sulfate fraction. The data indicate that the mechanisms of aggregation of human and rabbit platelets by SJAMP are different. THe SJAMP-induced human platelet aggregation is dependent upon metabolism, release of ADP and the cyclooxygenase pathway requiring fibrinogen and Ca++. The aggregation of rabbit platelets induced by SJAMP is independent of metabolism, release of ADP and cyclooxygenase pathway, and does not require fibrinogen and Ca++, but needs certain protein(s) in the 50 to 60% saturated ammonium sulfate fraction of rabbit plasma.

Glyoxal in Aqueous Ammonium Sulfate Solutions: Products, Kinetics and Hydration Effects

2011 ◽  
Vol 45 (15) ◽  
pp. 6336-6342 ◽  
Author(s):  
Ge Yu ◽  
Amanda R. Bayer ◽  
Melissa M. Galloway ◽  
Kyle J. Korshavn ◽  
Charles G. Fry ◽  
...  
Keyword(s):  
Ammonium Sulfate ◽  
Sulfate Solutions

Dissolution Kinetics of Ulexite in Ammonium Sulfate Solutions

2003 ◽  
Vol 42 (5) ◽  
pp. 982-986 ◽  
Author(s):  
Asım Künkül ◽  
Nizamettin Demirkıran ◽  
Ahmet Baysar
Keyword(s):  
Ammonium Sulfate ◽  
Dissolution Kinetics ◽  
Sulfate Solutions ◽  
Kinetics Of
Sign in / Sign up

Export Citation Format

Share Document