[Identification, purification and physico-chemical properties of neurospecific alpha 1-globulin].
The partially purified and concentrated 500-600-folds protein fraction has been obtained from human brain extract. This protein fraction was used for the immunization of rabbits. The corresponding anti-sera have the potency to detect the brain specific alpha 1-globulin, which is not identical to known cytoplasmatic brain specific protein. These antisera were used for the control of the antigen purification procedure which included ion-exchange, affinity and hydropho'ic chromatography, gel-filtration and isochromatofocusing. The antigen, purified to the homogeneity, has the electrophoretic mobility of the alpha 1-globulins, M(r) = 110-10 kD, and isoelectric point at pH 2.9-3.1.
Chekhonin
V P
VP
Morozov
S G
SG
Morozov
G V
GV
D000510:Alpha-Globulins / Q000737:chemistry / Q000302:isolation & purification*; D000596:Amino Acids / Q000032:analysis; D001923:Brain Chemistry; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003593:Cytoplasm / Q000737:chemistry; D004586:Electrophoresis; D006801:Humans; D009419:Nerve Tissue Proteins / Q000302:isolation & purification*
D000510:Alpha-Globulins; D000596:Amino Acids; D009419:Nerve Tissue Proteins