Bernard F. McKenzie

A STUDY OF CEREBRAL PROTEIN AND POLYSACCHARIDE IN THE DOG. III. "ALBUMIN" CHANGES IN EXPERIMENTAL CEREBRAL EDEMA.

I N PREVIOUS COMMUNICATIONS1.2 we reported on the normal cerebral protein and polysaccharide in dog brain. An increase in the relative concentration of albumin in cerebral edema was first noted by Kaps% in 1954. Sperl and associates4 developed a technic, using intracerebral implantation of psyllium seed, for consistentlv producing cerebral edema in the dog. Utilizing this technic, we have confirmed the finding of Kaps in experimental cerebral edema and are reporting an extension of this as a quantitative measure of cerebral edema.

Zone Electrophoretic Studies of Proteins and Glycoproteins of Bovine Serum and Synovial Fluid

Summary 1) Zone electrophoresis of 13 bovine sera yielded a mean concentration of 3.37 ± .29 g (42%) albumin, 1.19 ± .10 g (15%) alpha globulin, 1.23 ± .15 g (15%) beta globulin and 2.28 ± .49 g (28%) gamma globulin/100 ml. Serum protein-bound hexose was 124 mg/100 ml or 1.53 ± .12% of the mean serum protein concentration of 8.08 g/100 ml. Zone electrophoretic separation showed albumin to contain 7 ± 4%, alpha globulins 51 ± 6%, beta globulins 23 ± 4% and gamma globulins 20 ± 5% of the protein-bound polysaccharide. 2) Twenty-one synovial fluids from the same animals had a mean concentration of .90 ± .27 g (50%) albumin, .24 ± .08 g (14%) alpha globulins, .29 ± .10 g (16%) beta globulins and .37 ± .11 g (21%) gamma globulin/100 ml. Synovial fluid protein-bound hexose was 36 ± 11 mg/100 ml or 1.98 ± .46% of the mean synovial fluid protein of 1.80 g/100 ml. Zone electrophoretic separation showed albumin to contain 10 ± 5%, alpha globulins 49 ± 8%, beta globulins 28 ± 5%, and gamma globulins 14 ± 4% of the protein-bound polysaccharide. 3) The synovial fluid had relatively more albumin (50%) and relatively less gamma globulin (21%) than serum (albumin 42%, gamma globulin 28%) and a higher hexose/protein (PR) ratio indicating preferential permeability of albumin and one or more glycoproteins. Alpha globulins were not separated into alpha 1 and alpha 2 zones.