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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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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
1974
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC388266/ https://ncbi.nlm.nih.gov/pubmed/4208551 |
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