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XB-ART-28041
EMBO J. August 1, 1987; 6 (8): 2409-13.

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

Mattaj IW , Coppard NJ , Brown RS , Clark BF , De Robertis EM .


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.

PubMed ID: 2444435
PMC ID: PMC553647
Article link:

Genes referenced: eef1a1


References:
Brown, 1968, Pubmed[+]


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