נגישות
menu      
חיפוש מתקדם
תחביר
חפש...
הספר "אוצר וולקני"
אודות
תנאי שימוש
ניהול
קהילה:
אסיף מאגר המחקר החקלאי
פותח על ידי קלירמאש פתרונות בע"מ -
Effect of salicylhydroxamic acid (SHAM) on DL-DOPA oxidation by mushroom tyrosinase and by NaIO4
Year:
2000
Source of publication :
Journal of Food Biochemistry
Authors :
זקין, ורדה
;
.
כהן, ורדה
;
.
Volume :
24
Co-Authors:
Kahn, V., Department of Food Science, Agricultural Research Organization, Volcani Center, PO Box 6, Bet Dagan 50250, Israel
Zakin, V., Department of Food Science, Agricultural Research Organization, Volcani Center, PO Box 6, Bet Dagan 50250, Israel
Facilitators :
From page:
399
To page:
415
(
Total pages:
17
)
Abstract:
Salicylhydroxamic acid (SHAM) inhibits very effectively the rate of DL-DOPA oxidation by mushroom tyrosinase. SHAM also affects the spectrum of the initial product(s) formed when DL-DOPA is oxidized by mushroom tyrosinase or by NaIO4. Moreover, at certain concentrations, SHAM prevents the polymerization of dopaquinone formed enzymatically or nonenzymatically probably due to a chemical interaction between dopaquinone and SHAM.
Note:
Related Files :
עוד תגיות
תוכן קשור
More details
DOI :
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
19804
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:31
You may also be interested in
Scientific Publication
Effect of salicylhydroxamic acid (SHAM) on DL-DOPA oxidation by mushroom tyrosinase and by NaIO4
24
Kahn, V., Department of Food Science, Agricultural Research Organization, Volcani Center, PO Box 6, Bet Dagan 50250, Israel
Zakin, V., Department of Food Science, Agricultural Research Organization, Volcani Center, PO Box 6, Bet Dagan 50250, Israel
Effect of salicylhydroxamic acid (SHAM) on DL-DOPA oxidation by mushroom tyrosinase and by NaIO4
Salicylhydroxamic acid (SHAM) inhibits very effectively the rate of DL-DOPA oxidation by mushroom tyrosinase. SHAM also affects the spectrum of the initial product(s) formed when DL-DOPA is oxidized by mushroom tyrosinase or by NaIO4. Moreover, at certain concentrations, SHAM prevents the polymerization of dopaquinone formed enzymatically or nonenzymatically probably due to a chemical interaction between dopaquinone and SHAM.
Scientific Publication
You may also be interested in