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KMID : 0382619870070020797
Hanyang Journal of Medicine
1987 Volume.7 No. 2 p.797 ~ p.811
Purification and Characterization of Proteins and Ribonucleases Specific to Osteosarcoma




Abstract
Activities of ribonucleases (RNases) in tissue extracts of osteosarcoma were deter-mined and were compared with those of control tissue. RNases and proteins in both osteosarcoma and control tissues were isolated and characterized by DEAE-cellulose column chromatography, high performance liquid chromatography (HPLC) and polyacrylamide gel electrophoresis (PAGE) to find out the presence of the enzyme and proteins specific to the sarcoma.
1. Activities of both neutral and acid RNases were greatly increased in the tumor tissue of osteosarcoma, and the positive rates of tissue RNases as a tumor marker were significantly high in osteosarcoma.
2. Proteins and RNases in osteosarcoma tissue were fractionated into five peaks by a DEAE-cellulose columnn chromatography, of which two peaks appeared to be unique to the sarcoma. Two peak fractions for proteins and RNases observed in the control tissue were absent in the sarcoma tissue.
3. Among the electrophoretic (native-and SDS-PAGE) patterns of DEAE peak pro-teins common to osteosarcoma and control, the patterns of osteosarcoma were similar to those of control in the peak. V proteins, but different from those of con-trol in the peaks I and IV proteins.
4. DEAE peak I proteins from osteosarcoma tissue were subdivided into 7 peaks by HPLC, three of them being specific to osteosarcoma. One of the sarcoma specific protein peaks (HPLC peak 2 proteins) exhbited RNase activity.
Results obtained by this study suggested that the tumor specific proteins and RNases in the osteosarcomaa tissue appeared to be multiple in nature and that some of normal proteins were absent in the sarcoma tissues.
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