Of globulin

An equal volume of saturated ammonium sulphate solution is added to enable complete precipitation of globulin-bound chlordiazepoxide 14C,... 

The third test of protein homogeneity, developments from which remain in common use, was that of electrophoresis. Arne Tiselius had been a research assistant in Svedberg s laboratory. From 1925 he pioneered the application of electrophoresis to the analysis and separation of protein mixtures, showing with dialyzed serum differences in mobility of the protein components and the presence of three classes of globulins, a, B, and y. 

Discontinuities are seen in the relationship between increase in film pressure, An, and lipid composition following the injection of globulin under monolayers of lecithin-dihydro-ceramide lactoside and lecithin-cholesterol mixtures. The breaks occur at 80 mole % C 16-dihydrocaramide lactoside and 50 mole % cholesterol. Between 0 and 80 mole % lactoside and between 0 and 50 mole % cholesterol the mixed films behave as pure lecithin. Two possible explanations are the formation of complexes, having molar ratios of lecithin-lactoside 1 to 4 and lecithin-cholesterol 1 to 1 and/or the effect of monolayer configurations (surface micelles). In this model, lecithin is at the periphery of the surface micelle and shields the other lipid from interaction with globulin. 

With this model one might predict that when the lactose moiety is responsible for a specific interaction with protein (as in interaction with antibody directed against lactose), binding of the specific protein to the lactose would block its further penetration into the intermicellar (interlecithin) spaces. Experiments in which a specific antilactoside antibody was used in place of globulin (unpublished data) showed that this was indeed the case. The All value was much smaller than with nonspecific... 

Fig. 5. In the beginning of the run the evaporation flow pushes the unseparated fractions from the application zone (S) toward the center of the strip (2 hours). After 4 hours there is some opposite migration of globulins, and albumin progresses only slowly as they get nearer their immobilization points (6 hours).

For clinical purposes serum is preferable to plasma because the fibrinogen band interferes with the reading of globulin fractions. Moreover, it is easier to get serum free from traces of hemoglobin liberated by hemolysis. 

Wahba, A., El-Hagarawy, I.S., Zeidan, I.A. 1977. The effect of addition of globulin protein fractions on the creaming of buffaloes and cow s milk. Egypt. J. Dairy Sci. 5, 43—46. Walstra, P. 1967. On the crystallization habit in milk fat globules. Neth. Milk Dairy J. 21, 166-191. 

Malaekeh, M., Baradaran, H., Balali, M. (1991). Evaluation of globulin and immunoglobulins in serum of victims of chemical warfare in late phase of intoxication with sulfur mustard. In 2nd Congress of Toxicology, University of Tabrize Press, Tabrize. 

Passive immunity can be obtained by i.m. injection of globulin containing antibody to the virus normal immunoglobulin prepared from pooled plasma from known immune donors) which confers temporary protection for travellers visiting areas where the virus is endemic. Active immunisation with Hepatitis A vaccine is now preferable protective antibody takes about two weeks to develop. 

Albumin is synthesized in the liver cell. The rate of synthesis is 12—17 g/day (150-250 mg/kg BW), which can be enhanced 3—4 times due to a loss of albumin. The albumin pool of the organism is approx. 500 g. Half-life is 18—21 days. Albumin is determined as a part of serum electrophoresis either quantitatively (g/l or g/dl, respectively) or as a relative percentage (rel. %). Concentrations of globulins are also quantified in this way. 

Chloride ions react with undissociated mercuric thiocyanate to form undissociated mercuric chloride and free thiocyanate ions. The thiocyanate ions react with ferric ion (Fe " ") to form the highly colored, reddish complex of ferric thiocyanate with an absorption peak at 480 nm. Perchloric acid increases the intensity of the red color. High concentrations of globulins in the serum interfere in these methods because turbidity develops. This reaction is also very temperature sensitive. 

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