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. 1987 Aug;6(8):2409–2413. doi: 10.1002/j.1460-2075.1987.tb02519.x

42S p48--the most abundant protein in previtellogenic Xenopus oocytes--resembles elongation factor 1 alpha structurally and functionally.

I W Mattaj 1, N J Coppard 1, R S Brown 1, B F Clark 1, E M De Robertis 1
PMCID: PMC553647  PMID: 2444435

Abstract

We have undertaken an immunological and biochemical analysis of the most abundant soluble protein of previtellogenic Xenopus oocytes, 42S p48. We show that this protein shares immunological cross-reactivity with elongation factor 1 alpha (EF-1 alpha). Direct assays of both 42S fractions and purified 42S p48 show that this cross-reactivity is of functional significance since 42S p48, like EF-1 alpha, can transfer charged amino acids to ribosomes. We further demonstrate that 42S p48 is degraded soon after the onset of vitellogenesis, while the EF-1 alpha concentration remains essentially unchanged during this transition. These properties of 42S p48 are discussed with regard to its role in oogenesis.

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