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- W2023190034 abstract "This study concerns the nature of the fragments produced by pepsin digestion of human IgA1 myeloma proteins. The results show that pepsin digestion of IgA begins at the C-terminal end of the molecule and progress in several steps, leading to the formation of stable fragments. The first fragment obtained, called F(abc)′2α, corresponds to a monimeric IgA molecule which has lost its CH3 domain. It has a 140,000 dalton mol. wt and is made up of two light chains and two parts of heavy chain (mol. wt 45,000 daltons). The F(abc)′2α fragment is gradually digested and transformed into F(abc)′2α fragment (mol. wt 110,000 daltons). In the case of some senstive IgA proteins, a monomeric F(abc)′α fragment is also produced. The results also indicate that polymeric IgA proteins are more resistant to pepsin than monomeric IgA proteins." @default.
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- W2023190034 date "1977-01-01" @default.
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- W2023190034 title "Enzymatic fragmentation of human IgA F(abc)′2: A new peptic fragment" @default.
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- W2023190034 doi "https://doi.org/10.1016/0019-2791(77)90336-6" @default.
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