53620-20-5Relevant academic research and scientific papers
Isolation and characterization of a cysteine protease of freesia corms
Uchikoba, Tetsuya,Okubo, Michiko,Arima, Kazunari,Yonezawa, Hiroo
, p. 448 - 452 (2002)
A protease, freesia protease (FP)-A, was purified to electrophoretic homogeneity from regular freesia (Freesia reflacta) corms in harvest time. The Mr of FP-A was estimated to be 24 k by SDS-PAGE. The optimum pH of the enzyme was 8.0 using a casein substrate. These enzymes were strongly inhibited by p-chloromer-curibenzoic acid but not by phenylmethane- sulfonylfluoride and EDTA. These results indicate that FP-A belongs to the cysteine proteases. The amino terminal sequence of FP-A was similar to that of papain, and the sequences was regarded to the conservative residues of cysteine protease. From the hydrolysis of peptidyl-p-NAs, the specificity of FP-A was found to be broad. It was thought that FP-A was a new protease from freesia corms.
