[Characteristics of various nerve tissue proteins using group-specific sorbents].
The use of micro-scale column chromatography and affinity immunoelectrophoresis with group-specific sorbents allows studying some physical and chemical properties of protein molecules. A comparison of properties of soluble and membrane brain amino-peptidases carried out by means of micro-scale phenyl-sepharose and ConA-sepharose column chromatography shows that the membrane-bound aminopeptidase is a glycoprotein which possesses a high capacity to hydrophobic interactions. Soluble forms of aminopeptidase do not interact with ConA or phenyl residues. The crossed affinity immunoelectrophoresis in the presence of phenyl-sepharose also shows the presence of hydrophobic domains on the surface of glial fibrillary acidic protein molecules. The both approaches may be useful to predict conditions for large-scale affinity chromatography methods of protein and enzyme purification.
D000626:Aminopeptidases / Q000032:analysis; D000818:Animals; D002415:Cats; D002540:Cerebral Cortex / Q000201:enzymology; D002852:Chromatography, Ion Exchange; D005904:Glial Fibrillary Acidic Protein / Q000032:analysis; D007123:Immunoelectrophoresis, Two-Dimensional; D007164:Immunosorbents; D008566:Membranes / Q000201:enzymology; D009419:Nerve Tissue Proteins / Q000032:analysis*
D005904:Glial Fibrillary Acidic Protein; D007164:Immunosorbents; D009419:Nerve Tissue Proteins; D000626:Aminopeptidases
Kharakteristika nekotorykh belkov nervnoĭ tkani s primeneniem gruppospetsifichnykh sorbentov.