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The primer specificity of cytoplasmic poly(A) polymerase from cryptobiotic gastrulae of Artemia salina
Roggen, E.; Dams, E.; Slegers, H. (1985). The primer specificity of cytoplasmic poly(A) polymerase from cryptobiotic gastrulae of Artemia salina. Biochim. Biophys. Acta 825(1): 21-29. dx.doi.org/10.1016/0167-4781(85)90075-2
In: Biochimica et Biophysica Acta. Elsevier: Amsterdam. ISSN 0006-3002, more
Peer reviewed article  

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Author keywords
    Poly(A) polymerase; Primer specificity; (Artemia)

Authors  Top 
  • Roggen, E.
  • Dams, E.
  • Slegers, H.

Abstract
    Poly(A) polymerase has been purified to near homogeneity from the cytoplasm of Artemia salina as described previously (Roggen, E and Slegers, H. (1985) Eur. J. Biochem. 147, 225–232). Affinity chromatography on poly(A)-Sepharose 4B separates the enzyme preparation into two fractions. In standard assay conditions poly(A) polymerase fraction I (poly(A)-Sepharose 4B unbound) and fraction II (poly(A)-Sepharose 4B bound) have specific activities of 2.4 and 8.0 μmol AMP/h per mg enzyme, respectively. Poly(A) polymerase fraction II shows a high primer specificity towards the 17 S poly(A)-containing mRNP. Depending on the reaction conditions used, poly(A) sequences of 140 ± 15 AMP residues/μg enzyme are synthesized on the latter primer. In contrast, poly(A) polymerase fraction I only elongates oligo(A) primers efficiently. An endogenous RNA is detected in poly(A) polymerase II preparations. This RNA has a length of 83 ± 2 nucleotides and is a component of a 60 kDa particle. After removal of the latter the specificity of poly(A) polymerase fraction II for the 17 S poly(A)-containing mRNP is abolished and the characteristics of the enzyme resemble those of poly(A) polymerase I.

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