Spermidine is bound to a unique protein in early sea urchin embryos
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 (/sup 3/H)-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.
- OSTI ID:
- 5810792
- Journal Information:
- Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 22
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
SPERMIDINE
BIOCHEMICAL REACTION KINETICS
EMBRYOS
MOLECULAR WEIGHT
ONTOGENESIS
PROTEINS
SEA URCHINS
TRACER TECHNIQUES
TRITIUM COMPOUNDS
AMINES
ANIMALS
AQUATIC ORGANISMS
ECHINODERMS
INVERTEBRATES
ISOTOPE APPLICATIONS
KINETICS
LABELLED COMPOUNDS
ORGANIC COMPOUNDS
REACTION KINETICS
550201* - Biochemistry- Tracer Techniques