ISSN:
0022-3832
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
,
Physics
Notes:
By treating potato juice with acid it was found that potato globulin is converted to albumin and an insoluble casein-like protein. Potato albumin, salted out with ammonium sulfate and purified by dialysis, is very similar to ovalbumin; it is reconverted into a globulin-like protein by alkali. Solutions of potato albumin in water, as well as in acids and alkali, have a very low viscosity. Alkaline solutions of globulin have a greater viscosity than those of albumin; the viscosity numbers of the difficulty soluble protein are even greater. On the basis of the viscosity data, it was concluded that the albumin particles are corpuscular, the globulin molecules are longitudinal, and that the dissymetry is greatest for the difficulty soluble protein particles. On the basis of the different solubilities of all three proteins (which apparently have approximately the same chemical composition), it was concluded that the albumin molecule was the smallest and the difficulty soluble protein molecule the largest. An aqueous solution of potato albumin is denatured when heated to 50-60°, the viscosity thereby increasing more than 100-fold. The solutions become only slightly turbid, but do not flocculate. This unusual viscosity rise can be explained by the transformation of globular albumin molecules into fibrous, elongated particles. Only a slight viscosity increase is observed when alkaline solutions of albumin are heated. Albumin, in the presence of small amounts of salt, is precipitated at 50-60°; the salts also lower the turbidity point. However, very small concentrations of calcium chloride have a stabilizing effect. Albumin is not coagulated at room temperature by 1-2 N salt solutions. The experiments on the effect of cold on potato albumin showed that albumin, after congealing and thawing out, was more easily precipitated than the control solution. The viscosity of the cold-damaged albumin was somewhat less than that of the control solution. It was ascertained that the deaminated product of potato albumin was very similar to deaminated ovalbumin (solutions of high viscosity; linear colloid).
Additional Material:
10 Tab.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/pol.1946.120010606
