Abstract
The main sulfated proteins secreted by rabbit mammary gland tissue had M r of ∼67 000, 63 000 and 23 000, and one component which most likely corresponded to proteoglycans had a diffuse electrophoretic mobility ( M r>200 000). The sulfate groups in the 67–63 kDa proteins were mostly linked to carbohydrates. These proteins and the 23 kDa protein were co-purified and identified to heavy chains of immunoglobulin A (IgA) and J chain, respectively. Sulfation of α-chains also occurred in rat mammary and rabbit lacrimal glands. We conclude that polymeric IgA which are produced by plasma cells and released in secretion fluids after transcytosis through epithelia are sulfated.
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