G-globulin

Pandurangi, R.S. et al. (1995b) High efficiency photolabeling of human serum albumin and human g-globulin with [14C]Methyl 4-azido-2,3,5,6-tetrafluorobenzoate. Bioconjugate Chem. 6, 630-634. 

ForsgrenA, SjoquistX. ProteinA fromS. aureus. I. pseudo immunoreactionwith human g-globulin. J Immunol 1966 97 822-827. 

L4. Lichtman, M. A., Vaughan, J. H., and Hames, G. G., The distribution of serum immunoglobulins, anti G globulins (rheumatoid factors) and anti nuclear antibodies in white and negro subjects in Evans County, Georgia. Arthritis Rheum. 10, 204-215 (1967). 

Hellsing K. Immune reactions in polysaccharide media I. The effect of dextran on the reaction between ff-iabeled human serum albumin and gamma-G-globulin from rabbit. Acta Chem Scand 1966 20 1251-62. 

H6. Harboe, M., Pande, H., Brandtzaeg, P., Tveter, K. J., and Hjort, P. F., Synthesis of donor type gamma-G-globulin following thymus transplantation in hypo-gamma-globulinaemia with severe lymphocytopenia. Scand. J. Haematol. 3, 351-374 (1966). 

Since this paper went to press a noteworthy publication by J. W. L. Davies, S.-O. Liljedahl, and G. Birke has appeared in Injury, 1, 43 (1969). Nineteen patients with bums of varying sizes were treated in a warm (32°C), dry environment and another group of 41 with similar sized bums in a cooler (22°C), more moist environment. Those in the warm, dry environment showed smaller losses of body weight while in the hospital, with significant reductions in basal metabolic rate and the rate of catabolism of plasma albumin and y-G-globulin, smaller amounts of protein in the extravascular space, increased serum albumin concentrations, a greater rate of synthesis of albumin, and a lower rate of synthesis of y-G-globulin. Less protein was lost in the exudate when the patients were exposed in the warm, dry environment and their clinical condition was often better than those in the normal hospital environment. 

Polystyrene beads are known for their capacity to bind immunoglobin G globulins nonspecifically, by hydrophobic interaction, so that the immu-nospecificity of the Fab region is preserved. Because of the dipolar nature of the phenyl ring, polystyrene probably represents a surface capable of extraordinary interaction with hydrophobic regions of proteins. 

Figure 16. The separation of >-G globulin and Ampholine. The sample was in a volume of 12 ml of 25% sucrose (w/v). The column was 2.5 X 20 cm and the bed Sephadex G-50 (tine). Sample volume 6 ml. Eluant 0.1 M imidazolacetate buffer pH 7. F ow rate 72 mlA (Vesterberg, 50).

Fig.3. Sedimentation pattern of normal human serum in the ultracentrifuge, measured with a schlieren optical system. Left hand picture taken 51 min after start of centrifugation right hand picture after 125 min. Centrifugation at 59,800 rpm. A albumin, 4.5S G = globulin, 7S M = macroglobulin, 19S.

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