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Plant and Cell Physiology, 1986, Vol. 27, No. 6 1043-1050
© 1986

Article

Further Biochemical Characterization of a Cell Fusion Hormone from the Red Alga, Griffithsia pacifica

Bruce A. Watson1 and Susan D. Waaland2

1Department of Botany, University of Washington Seattle, Washington 98195, U.S.A.
2Department of Biology, University of Puget Sound Tacoma, Washington 98416, U.S.A.

In the marine red alga, Griffithsia pacifica, the repair process initiated upon death of an intercalary cell is mediated by a glycoprotein hormone, rhodomorphin. In this paper we show that the glycosidic portion of the molecule has terminal {alpha}-D-mannosyl residues which are at least in part responsible for the binding of rhodomorphin by concanavalin A. The protein portion of the molecule contains disulfide bridges. These bridges must be intact for biologically active hormone to be recovered from a denatured state. Isolation of active rhodomorphin from SDS-PAGE indicates a molecular weight of 15,000–17,500. This agrees well with our previously published [Watson and Waaland (1983) Plant Physiol. 71: 327] molecular weight from gel filtration of 14,000.

(Received February 26, 1986; Accepted June 2, 1986)
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