Association of melanoma tumor antigen activity with β 2-microglobulin

A. Malley; D. R. Burger; A. A. Vandenbark; M. Frikke; P. Finke; D. Begley; K. Acott; J. Black; R. M. Vetto

Association of melanoma tumor antigen activity with β ₂-microglobulin

A. Malley, D. R. Burger, A. A. Vandenbark, M. Frikke, P. Finke, D. Begley, K. Acott, J. Black, R. M. Vetto

Neurology

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

The majority of melanoma tumor antigen activity present in melanoma extracts derived from fresh tumor tissue binds to a Sepharose-anti-β2-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 Sepharose-anti-β2-microglobulin adsorbent. The complete blocking of MTA activity by pretreating the anti-β2-microglobulin adsorbent with β2-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-β2-microglobulin adsorbent.

Original language	English (US)
Pages (from-to)	619-623
Number of pages	5
Journal	Cancer Research
Volume	39
Issue number	2 II
State	Published - 1979

ASJC Scopus subject areas

Oncology
Cancer Research

Cite this

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title = "Association of melanoma tumor antigen activity with β 2-microglobulin",

abstract = "The majority of melanoma tumor antigen activity present in melanoma extracts derived from fresh tumor tissue binds to a Sepharose-anti-β2-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 Sepharose-anti-β2-microglobulin adsorbent. The complete blocking of MTA activity by pretreating the anti-β2-microglobulin adsorbent with β2-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-β2-microglobulin adsorbent.",

author = "A. Malley and Burger, {D. R.} and Vandenbark, {A. A.} and M. Frikke and P. Finke and D. Begley and K. Acott and J. Black and Vetto, {R. M.}",

year = "1979",

language = "English (US)",

volume = "39",

pages = "619--623",

journal = "Cancer Research",

issn = "0008-5472",

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T1 - Association of melanoma tumor antigen activity with β 2-microglobulin

AU - Malley, A.

AU - Burger, D. R.

AU - Vandenbark, A. A.

AU - Frikke, M.

AU - Finke, P.

AU - Begley, D.

AU - Acott, K.

AU - Black, J.

AU - Vetto, R. M.

PY - 1979

Y1 - 1979

N2 - The majority of melanoma tumor antigen activity present in melanoma extracts derived from fresh tumor tissue binds to a Sepharose-anti-β2-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 Sepharose-anti-β2-microglobulin adsorbent. The complete blocking of MTA activity by pretreating the anti-β2-microglobulin adsorbent with β2-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-β2-microglobulin adsorbent.

AB - The majority of melanoma tumor antigen activity present in melanoma extracts derived from fresh tumor tissue binds to a Sepharose-anti-β2-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 Sepharose-anti-β2-microglobulin adsorbent. The complete blocking of MTA activity by pretreating the anti-β2-microglobulin adsorbent with β2-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-β2-microglobulin adsorbent.

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AN - SCOPUS:0018341348

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JO - Cancer Research

JF - Cancer Research

IS - 2 II

ER -

Association of melanoma tumor antigen activity with β ₂-microglobulin

Abstract

ASJC Scopus subject areas

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