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  • Title: 42S p48--the most abundant protein in previtellogenic Xenopus oocytes--resembles elongation factor 1 alpha structurally and functionally.
    Author: Mattaj IW, Coppard NJ, Brown RS, Clark BF, De Robertis EM.
    Journal: EMBO J; 1987 Aug; 6(8):2409-13. PubMed ID: 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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