| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Department of Immune Diseases, Oregon Regional Primate Research Center, Beaverton, Oregon 97005 [A. M., M. F., D. B.]; Surgical Research Laboratory, Veterans Administration Hospital, Portland, Oregon 97201 [D. R. B., A. A. V., P. F., R. M. V.]; and Departments of Microbiology and Immunology [D. R. B., A. A. V.], Surgery [D. R. B., R. M. V.], and Biochemistry [K. A., J. B.], University of Oregon Health Science Center, Portland, Oregon 97207
The majority of melanoma tumor antigen activity present in melanoma extracts derived from fresh tumor tissue binds to a Sepharose-anti-ß2-microglobulin adsorbent. Removal of HLA antigens from the extracts of melanoma tissue by using a KBr flotation technique did not reduce either the tumor antigen activity of the extracts or the binding of melanoma tumor antigen (MTA) activity to the Sepharoseanti-ß2-microglobulin adsorbent. The complete blocking of MTA activity by pretreating the anti-ß2-microglobulin adsorbent with ß2-microglobulin and the lack of detectable MTA binding to a Sepharose anti-normal human serum adsorbent demonstrated the specificity of the binding of MTA to the anti-ß2-microglobulin adsorbent.
1 Presented at the International Workshop on Leukocyte Adherence Inhibition, May 15 to 17, 1978, Buffalo, N. Y. Publication No. 0000 of the Oregon Regional Primate Research Center. Supported by USPHS Contract NO1-CB53954 from the Division of Cancer Biology and Diagnosis, National Cancer Institute.
2 To whom requests for reprints should be addressed.
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Cancer Research | Clinical Cancer Research |
| Cancer Epidemiology Biomarkers & Prevention | Molecular Cancer Therapeutics |
| Molecular Cancer Research | Cancer Prevention Research |
| Cancer Prevention Journals Portal | Cancer Reviews Online |
| Annual Meeting Education Book | Meeting Abstracts Online |