Purification and characterization of invertase inhibitors from Dioscorea rotundata tuber.
Three invertase inhibitors (A), (B) and (C) from Dioscorea rotundata tuber were resolved on DEAE-cellulose ion exchanger. Two of the inhibitors, (B) and (C), were proteins and homogenous on polyacrylamide gels Mr 21,000 +/- 85 and 26,982 +/- 40/36,307 +/- 50 respectively. The inhibitors (B) and (C) were inactivated at 60 degrees C and had activity-pH optima at 5.2 and 6.4 respectively. (B) and (C) were non competitive inhibitors of invertase from yam and other sources.
Nok
A J
AJ
Department of Biochemistry, Ahmadu Bello University, Zaria, Nigeria.
Igwe
U A
UA
Pai
S J
SJ
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D004791:Enzyme Inhibitors / Q000302:isolation & purification* / Q000494:pharmacology; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors*; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D009492:Neurospora crassa / Q000201:enzymology; D010944:Plants / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D011198:Solanum tuberosum / Q000201:enzymology; D013552:Swine; D013816:Thermodynamics; D014675:Vegetables / Q000737:chemistry*; D043324:beta-Fructofuranosidase
D004791:Enzyme Inhibitors; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase