Kinetic studies on inhibition of aminopropyltransferases by aurintricarboxylic acid in vitro

Chemico-biological Interactions
H HibasamiJ Nagai

Abstract

Activities of aminopropyltransferases (spermidine synthase and spermine synthase) were inhibited by aurintricarboxylic acid (ATA). Spermidine synthase was slightly more sensitive to the inhibitor than spermine synthase. These inhibitions were not prevented by 0.15 M NaCl. Inhibition by ATA of spermidine synthase was 'uncompetitive' with respect to putrescine and that of spermine synthase was 'non-competitive' with respect to spermidine. When the amount of spermidine synthase or spermine synthase was varied, inhibition ratio hardly changed on either case implying no appreciable interaction between ATA and these enzymes.

References

Mar 1, 1978·The Biochemical Journal·H Hibasami, A E Pegg
Dec 10, 1973·Biochemical and Biophysical Research Communications·T Blumenthal, T A Landers
Oct 1, 1968·Proceedings of the National Academy of Sciences of the United States of America·A P Grollman, M L Stewart
Jan 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·M L StewartM T Huang

Citations

Aug 1, 1995·Immunological Reviews·K S Sellins, J J Cohen
Mar 4, 2008·Genome Biology·Alena A AntipovaTodd R Golub

Related Concepts

Metazoa
Aurintricarboxylic Acid, Calcium (2: 3) Salt
Cyclohexanecarboxylic Acids
Spermidine Synthase
Putrescine
Sodium Chloride, (24)NaCl
Spermidine
Spermine Synthase
Transferase
Rats, Laboratory

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