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  • Title: Methionyl-tRNA synthetase from sheep mammary gland. Purification of a fully active monomeric enzyme derived from high-molecular-weight complexes by controlled proteolysis.
    Author: Kellermann O, Viel C, Waller JP.
    Journal: Eur J Biochem; 1978 Jul 17; 88(1):197-204. PubMed ID: 566665.
    Abstract:
    Methionyl-tRNA synthetase from sheep lactating mammary gland is found predominantly in the form of high-molecular-weight complexes. Controlled proteolysis of these aggregates generates a low-molecular-weight species of the enzyme with full maintenance of activity as assessed by the rate of aminoacylation of tRNA. The product of proteolysis, which has been purified to homogeneity with a yield of 23%, is a monomeric enzyme of molecular weight 78 000. It has a specific activity of 405 units/mg at 25 degrees C. These findings clearly demonstrate that the aggregated state of methionyl-tRNA synthetase is not a prerequisite for full expression of catalytic activity. Furthermore, the results emphasize the need to provide effective protection against proteolytic damage in studies dealing with the characterization of high-molecular-weight complexes of aminoacyl-tRNA synthetases.
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