Co-Authors:
Raccah, B., The Hebrew University, Rehovot Campus, Israel, Israel Institute for Biological Research, Ness-Ziona, Israel
Applebaum, S.W., The Hebrew University, Rehovot Campus, Israel, Israel Institute for Biological Research, Ness-Ziona, Israel
Tahori, A.S., The Hebrew University, Rehovot Campus, Israel, Israel Institute for Biological Research, Ness-Ziona, Israel
Abstract:
The kinetics of dihydrofolate reductase activity were determined in a post-mitochondrial supernatant of whole aphid homogenate. The apparent Kms for dihydrofolate and NADPH were found to be 2·6 × 10-7M and 11·5 × 10-6M respectively. Aminopterin inhibited activity of dihydrofolate reductase in vitro (Ki = 1·65-1·85 × 10-10 M). The properties of the aphid enzyme are compared to those of dihydrofolate reductase from other sources. © 1973.
תפריט נגישות
ניגודיות עדינה
מונוכרום
הדגשת קישורים
חסימת אנימציה
פונט קריא
סגור
איפוס הגדרות נגישות
להורדת מודול נגישות חינם
