Complete Amino Acid Sequence of a Papain-Solubilized Human Histocompatibility Antigen, HLA-B7. 1. Isolation and Amino Acid Composition of Fragments and of Tryptic and Chymotryptic Peptides

Jose A.López de Castro, Harry T. Orr, Richard J. Robb, Thomas G. Kostyk, Jack L. Strominger, Dean L. Mann

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Abstract

As a part of the overall strategy for determining the complete covalent structure of the papain-solubilized portion of the heavy chain of the human histocompatibility antigen H.LA-B7, the protein was dissected into various fragments by a combination of partial acid hydrolysis and cyanogen bromide cleavage. After purification by chromatographic procedures, these fragments have been used as a source for tryptic and chymotryptic peptides, Thirty-three major tryptic and twenty-two major chymotryptic peptides were purified in nanomole amounts and their amino acid compositions determined. These peptides account for the whole extent of the polypeptide chain with the exception of the am-ino-terminal CNBr pentapeptide. They provide the basis for the formal alignment of the acid cleavage and cyanogen bromide fragments of the molecule as well as the source material for the elucidation of the primary structure of the HLA-B7 heavy chain.

Original languageEnglish (US)
Pages (from-to)5704-5711
Number of pages8
JournalBiochemistry
Volume18
Issue number25
DOIs
StatePublished - Jan 1 1979

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