Human spleen RNase was purified using an immunoabsorbent produced with anti human liver RNase serum. The purification was more rapid than the procedure used to purify the liver RNase, yet the final specific activity was similar. Problems encountered previously using immunoabsorbents to purify enzymes were to a large degree avoided by injecting only microgram amounts of human liver RNase directly into the popliteal lymph nodes of rabbits, thereby producing a low avidity antibody. The low avidity antibody permitted elution from the immunoabsorbent with only dilute citrate buffer and without significant denaturation. An examination of crude spleen homogenates did not reveal any other RNase to be present except that which bound to the antibody. The enzyme was found to be antigenically unrelated to the human plasma RNase. A comparison of the physical properties of the human spleen enzyme with those of the human liver enzyme did not reveal any significant differences.
|Original language||English (US)|
|Number of pages||7|
|Journal||Journal of Biological Chemistry|
|State||Published - 1976|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology