scholarly journals A Simple Method for Vacuum Extraction and Quantitative Determination of Internal Ethylene of Excised Apple Tissue

1994 ◽  
Vol 63 (2) ◽  
pp. 453-459 ◽  
Author(s):  
Tomonori Kawano ◽  
Keishi Shimokawa
2013 ◽  
Vol 2013 ◽  
pp. 1-3
Author(s):  
Suman K. Giri ◽  
Nigamananda Das

An easy and feasible approach to recover HgCl2, used in quantitative determination of iron values, as Hg(0) was described. Both Hg(I) and Hg(II), present in the solution after quantitative determination of iron, was completely reduced to Hg(0) by the addition of aluminium chips in more slightly excess than the stoichiometric amount. The purity of recovered Hg(0) was verified by comparing the value of density with pure mercury. This simple method may be useful to remove the mercury from other waste aqueous solutions before their discharge into the environment.


1933 ◽  
Vol 5 (1) ◽  
pp. 63-74 ◽  
Author(s):  
H. D. Kay ◽  
W. R. Graham

A method is described for the quantitative determination of phosphatase in raw milk. Using this method, it has been found that phosphatase is sufficiently thermolabile to be destroyed completely by pasteurisation if this process is properly carried out. The absence of phosphatase from a sample of milk or cream indicates with a fair degree of certainty that the milk or cream has been heated sufficiently to destroy such pathogenic organisms as were originally present, though it is of course no guarantee that the product is free from these organisms at the time of testing.A simple, qualitative test-tube method is described which may be used for differentiating between raw and heated milk, or between raw and heated cream, and which with slight modifications may also be used for distinguishing between butters made from raw or from heated cream.


1966 ◽  
Vol 15 (03/04) ◽  
pp. 511-518
Author(s):  
W Berg ◽  
K Korsan-Bengtsen ◽  
J Ygge

SummaryA simple method for preparation of plasminogen with low spontaneous activity and soluble at a neutral pH and at physiological ionic strength is described. Euglobulin made from fresh, oxalated, BaSO4-adsorbed, human plasma was first purified by means of gel filtration on Sephadex G-200. After gel filtration, further purification and concentration was done on DEAE-sephadex A-50. The activity was 100-130 casein units per mg tyrosine.


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