The different electrophoretic forms of post gamma-globulin their antigenic identity and their structural variability.
Post gamma-globulin, first described as a constant component of protein of cerebrospinal fluid and urine from patients with tubular disorders has also been found in other biological fluids. Post gamma-globulin from a single individual always migrated as several bands after storage. Three electrophoretic forms, immunochemically identical, have been isolated by gel chromatography, preparative continuous flow electrophoresis and ion-exchange chromatography. Their molecular weight was found to be approximately between 11 000 to 12 000. No difference between the three forms could be detected. The N-terminal amino acids were found to be Lys, Arg and Leu respectively for the three forms of post gamma-globulin. The "slow" and "fast" forms of post gamma-globulin seemed to differ by elimination of small basic peptides or amino acids from the N-terminal end of the protein. No enzymatic activity of post gamma-globulin was found, but this requires further investigations.
D000596:Amino Acids / Q000032:analysis; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes; D005916:Globulins / Q000134:cerebrospinal fluid / Q000276:immunology / Q000652:urine; D006801:Humans; D012712:Serum Globulins / Q000032:analysis / Q000276:immunology
D000596:Amino Acids; D000939:Epitopes; D005916:Globulins; D012712:Serum Globulins