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A Structural Study of Human Exocrine IgA Globulin

From the Rheumatism Research Wing, Department of Experimental Pathology The Medical School, University of Birmingham, Birmingham, England and The Children's Asthma Research Institute and Hospital, Denver, Colorado

Abstract

Exocrine A globulin was isolated from human colostrum in a pure state. Measurement of s⁰_20,w and d_20,w indicated a MW of about 393,000. Dissociation of the subunits of this 11.7 S molecule was effected by reduction and alkylation, with or without treatment with acid or sodium dodecyl sulfate. The results suggested that the 11.7 S exocrine A molecule comprises two molecules of monomer A globulin and one of secretory piece (SP) and is stabilized by both disulfide and noncovalent bonds. A protein was identified in normal colostrum with the same antigenic and size characteristics as the SP dissociated from exocrine A globulin. The MW of SP was estimated to be 76,000 on the basis of gel filtration data.

Footnotes

¹ Special Fellow, U.S.P.H.S. Partly supported by U.S.P.H.S. Grant 5501FR05523. Present address, C.A.R.I.H., 3401 West 19th Avenue, Denver, Colorado 80204, U.S.A.

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