Characterization of a large fragment produced by proteolysis of human immunoglobulin M with papain.

Abstract The controlled digestion of human immunoglobulin M (IgM) (Patient Dau.) with papain in the presence of 0.002 m mercaptoethylamine resulted in the release of a basic subunit-like fragment which we designated IgMp. It resembled the subunit (IgMs) produced by mild reduction of IgM in the following ways. The molecular weight (186,000) and sedimentation coefficient (6.2 to 6.5 S) of IgMp were similar to those of IgMs. IgMp contained light chains and a large portion of each of its µ chains. IgMp was antigenically identical with IgMs and IgM when tested with specific anti-IgM antiserum. The mobilities of IgMp and IgMs in agarose seemed to be virtually identical. In contrast, IgMp did not possess the free sulfhydryl groups which were found on IgMs. It was concluded that IgMp was formed from IgM by proteolysis of the µ chains near the carboxyl terminus. The fragment retained intact its interchain disulfide bonds.

• Publication year

  1968

• Venue

  Journal of Biological Chemistry

• Publication date

  1968-11-10

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/s0021-9258(18)91909-5PMID 4972432
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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