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. 1985 Nov;82(22):7613–7615. doi: 10.1073/pnas.82.22.7613

Spermidine is bound to a unique protein in early sea urchin embryos.

Z N Canellakis, P K Bondy, A A Infante
PMCID: PMC391383  PMID: 3865182

Abstract

Spermidine is rapidly taken up and becomes bound to protein during the very early hours of sea urchin embryogenesis. During the first 6 hr after fertilization of freshly obtained sea urchin eggs (Strongylocentrotus purpuratus), which are incubated in the presence of exogenous [3H]-spermidine, up to 7% of the total cell-associated spermidine appears uniquely as spermidine bound in macromolecular form. This unique protein containing spermidine migrates as a single radioactive band in gel electrophoresis. It has a Mr of approximately equal to 30,000 and is readily distinguishable from the protein initiation factor eIF-4D, which has a Mr of 18,000, the only other identifiable protein known to date to be posttranslationally modified by polyamines.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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