[Isolation and various properties of leucine aminopeptidase from biological fluids of patients with multiple sclerosis].
Specific form of leucine aminopeptidase (which was distinct from other forms of the enzyme found in blood) was characterized by its physico-chemical properties--pH optimum, substrate specificity, electrophoretic mobility and molecular mass. The enzyme was isolated from biological fluids of patients with multiple sclerosis. Free and bound forms of the enzyme were detected in blood and cerebrospinal fluid. Estimation of the bound enzyme activity has a diagnostic significance.
D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007931:Leucyl Aminopeptidase / Q000097:blood / Q000134:cerebrospinal fluid / Q000302:isolation & purification*; D008970:Molecular Weight; D009103:Multiple Sclerosis / Q000201:enzymology*; D009186:Myelin Sheath / Q000201:enzymology*; D013379:Substrate Specificity
D007931:Leucyl Aminopeptidase
Vydelenie i nekotorye svoĭstva spetsificheskoĭ leĭtsinaminopeptidaziz biologicheskikh zhidkosteĭ bol'nykh rasseiannym sklerozom.