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Neural cell adhesion molecule (NCAM) has been described as a family of membrane glycoproteins. However, soluble NCAM immunoreactivity has long been recognized. We here show that soluble NCAM is composed of two quantitatively major polypeptides of M r 180 000 and 115 000 and two minor components of M r 160 000 and 145 000. Soluble NCAM was immunochemically identical to membrane NCAM, was polysialylated and carried the HNK‐1 epitope. It only constituted 0.8% of total NCAM in newborn rat brain. Soluble NCAM appeared in neuronal cell culture medium 15–30 min after the start of synthesis preceding accumulation of membrane‐associated NCAM on the cell surface. This indicates that soluble NCAM contains a secreted component.

Background: AtBBX32 is a member of the B-box protein family from A. thaliana. Its molecular mechanism is poorly understood. Results: We demonstrate functional interactions of AtBBX32 with soybean BBX62 (GmBBX62). Conclusion:The N-terminal B-box domain plays a key role in mediating the interaction between AtBBX32 and GmBBX62. Significance: Our data offer novel insight into the role of B-box domains in mediating protein-protein interactions between different plant B-box proteins.

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