Purification and some properties of an aminopeptidase from the seeds of Cannabis sativa.
An aminopeptidase (HSA) with a molecular mass of 78 kDa was purified from hemp (Cannabis sativa) seeds. The activity was inhibited by monoiodeacetic acid, p-chloromercuri-phenylsulfonic acid, and Zn2+ ion. The specificity of HSA was similar to that of a leucyl aminopeptidase [EC 3.4.11.1] from mammalian cytosol. However, other enzyme properties were different from these of leucyl aminopeptidase.
Arima
K
K
Department of Chemistry, Faculty of Science, Kagoshima University, Korimoto, Japan.
Uchikoba
T
T
Shimada
M
M
Yonezawa
H
H
Kaneda
K
K
D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism*; D002188:Cannabis / Q000737:chemistry / Q000201:enzymology*; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D012639:Seeds / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature
D004791:Enzyme Inhibitors; D000626:Aminopeptidases