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PMID: 4208551 Published · ppublish English Journal Article

Partial purification of detergent-soluble HL-A antigen and its cleavage by papain.

Springer TA, Strominger JL, Mann D

Abstract

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 least two cleavages to a 34,000 MW peptide, but the 12,000 MW peptide appears to be unchanged. Concomitantly, the apparent molecular weight in gel filtration chromatography under nondenaturing conditions in the presence of Brij 99 is reduced from 460,000 to 45,000. HL-A molecules produced by direct papain proteolysis of membranes and by papain treatment of purified detergent-soluble HL-A are identical.

MeSH Terms
Animals Cell Line Chromatography, Affinity Chromatography, DEAE-Cellulose Chromatography, Gel Chromium Radioisotopes Detergents Edetic Acid Histocompatibility Antigens/isolation & purification Humans Hydrolysis Lymphocytes/immunology Mice Molecular Weight Papain Peptide Fragments/analysis Precipitin Tests Serum Albumin, Bovine Sodium Dodecyl Sulfate
Chemicals
Chromium Radioisotopes Detergents Histocompatibility Antigens Peptide Fragments Serum Albumin, Bovine Sodium Dodecyl Sulfate Edetic Acid Papain
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Springer T A
Strominger J L
Mann D
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35 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1974-04-00
Pages
1539-43
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC388266
Subset
IM
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