?NEGATIVE PURIFICATION OF THE PLASMA MEMBRANE ATPASE OF RHODOTORULA GLUTINIS

Authors

  • T A Kumosani Hughes Laboratories, Chemistry Department,MiamiUniversity, Oxford, OR 45056, USA
  • C C Griffin Biochemistry Department, Faculty of Science, Saudi Arabia POBox 9028, King Abdulaziz University,Jeddah 21413,

Keywords:

ATPase, Rhodotorula glutinis, Plasma membrane.

Abstract

The ATPase from the aerobic yeast Rhodotorula glutinis was purified by removing undesirable proteins. Four different
reagents proved effective in removing about 50% of undesirable proteins (peripheral membrane and/or cytoplasmic pro-
teins that might be trapped during membrane isolation). The plasma membrane suspensions were treated with KCI (2M),
followed by lysophosphatidylcholine (0.001 %, wv .1), then Triton (0.02%, wv .1) and finally deoxycholate (4 mM). This
resulted in removal of 50 % of the proteins while increasing the ATP ase activity 20% above the control level, resulting in
about 2.5-fold purification.

Downloads

Published

1999-12-20

How to Cite

Kumosani, T. A., & Griffin, C. C. (1999). ?NEGATIVE PURIFICATION OF THE PLASMA MEMBRANE ATPASE OF RHODOTORULA GLUTINIS. Biological Sciences - PJSIR, 42(6), 364–367. Retrieved from http://v2.pjsir.org/index.php/biological-sciences/article/view/2206

Issue

Vol. 42 No. 6 (1999): Pakistan Journal of Scientific and Industrial Research

Section

Articles