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Partial Purification of Detergent-Soluble HL-A Antigen and Its Cleavage by Papain

HL-A antigen solubilized with the non-ionic detergent, Brij 99, has been purified to about 50% of homogeneity from a cultured human lymphoblast line. It consists of two nonidentical subunits of 44,000 and 12,000 molecular weight (MW). Upon papain proteolysis the 44,000 MW peptide is converted by at...

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Main Authors: Springer, Timothy A., Strominger, Jack L., Mann, Dean
Format: Artigo
Jezik:Inglês
Izdano: 1974
Teme:
Online dostop:https://ncbi.nlm.nih.gov/pmc/articles/PMC388266/
https://ncbi.nlm.nih.gov/pubmed/4208551
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