[X-ray microanalysis of the activity of immobilized papain].
The localization of activity of immobilzed papain by covalent-binding was studied by X-ray microanalysis. N alpha-benzoyl-L-arginineamide hydrochloride and FeCl3 served as substrate and capturer respectively. Substrate was catalysed by immobilized papain to produce L-arginine and NH3. NH3 was captured by FeCl3 to form precipitate Fe(OH)3. Precipitation deposited was used to locate active site of immobilized papain. The results show that the macroporous resins carrier of immobilized papain leads to greater enzyme activity, and the distribution of activated enzyme is uniform. Most of activated enzyme was immobilized on the macroporous resins. The optimum condition of localization of activity of immobilized papain was studied.
Ding
Liang
L
Research Center of Physical and Chemical Analysis, Hebei University, Hebei Medical Continued Education College, Baoding 071002, China.
Yao
Zi-hua
ZH
Li
Tong
T
Qiu
Man-de
MD
D001120:Arginine / Q000031:analogs & derivatives* / Q000737:chemistry; D002712:Chlorides; D004577:Electron Probe Microanalysis / Q000379:methods; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005290:Ferric Compounds / Q000737:chemistry; D010206:Papain / Q000378:metabolism*; D013379:Substrate Specificity
D002712:Chlorides; D004800:Enzymes, Immobilized; D005290:Ferric Compounds; C029772:arginine beta-naphthylamide; D001120:Arginine; D010206:Papain; C024555:ferric chloride