Literature DB >> 2770710

Comparison of the thermolability and hydrophobic properties of high- and low-molecular-weight forms of rabbit liver arginyl-tRNA synthetase.

H Berbeć1, A Paszkowska.   

Abstract

Two preparations with arginyl-tRNA synthetase activity have been obtained from rabbit liver post-microsomal fraction: a) a high-molecular-weight containing the multienzyme aminoacyl-tRNA synthetase complex and b) a low-molecular-weight preparation containing free enzymes. Thermal inactivation of arginyl-tRNA synthetase in both preparations has been compared in a solution which was successively supplemented with tRNA, reduced glutathione, L-ascorbic acid, ZnCl2 and Triton X 100. Moreover, hydrophobic properties of both enzyme preparations have been compared. It was found that the complexed arginyl-tRNA synthetase is more stable than the free enzyme. A role of hydrophobic interactions in the maintenance of the complexed enzyme stability is suggested.

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Year:  1989        PMID： 2770710     DOI： 10.1007/BF00222612

Source DB:  PubMed          Journal:  Mol Cell Biochem        ISSN： 0300-8177            Impact factor:   3.396


  37 in total

1.  Subcellular localization of S-adenosyl-L-methionine:tRNA methyltransferases with aminoacyl-tRNA synthetases in human and mouse: normal and leukemic leukocytes.

Authors:  P F Agris; D K Woolverton; D Setzer
Journal:  Proc Natl Acad Sci U S A       Date:  1976-11       Impact factor: 11.205

2.  Metallothionein: a cadmium- and zinc-containing protein from equine renal cortex.

Authors:  J H KAGI; B L VALEE
Journal:  J Biol Chem       Date:  1960-12       Impact factor: 5.157

3.  Detection and partial purification of rapidly sedimenting forms of aminoacyl-transfer ribonucleic acid synthetases from human placenta.

Authors:  R M Denney
Journal:  Arch Biochem Biophys       Date:  1977-09       Impact factor: 4.013

4.  Studies on rat liver phenylalanyl transfer ribonucleic acid synthetase. II. Further purification, substrate specificity, and effects of substrates on heat inactivation.

Authors:  J S Tscherne; K W Lanks; P D Salim; D Grunberger; C R Cantor; I B Weinstein
Journal:  J Biol Chem       Date:  1973-06-10       Impact factor: 5.157

5.  Heavy and light forms of some aminoacyl-tRNA synthetases in fraction X, microsomes and cytosol of rabbit liver.

Authors:  H Berbeć; A Paszkowska; T Borkowski
Journal:  Mol Cell Biochem       Date:  1984-06       Impact factor: 3.396

6.  Binding of zinc to Escherichia coli phenylalanyl transfer ribonucleic acid synthetase. Comparison with other aminoacyl transfer ribonucleic acid synthetases.

Authors:  J F Mayaux; S Blanquet
Journal:  Biochemistry       Date:  1981-08-04       Impact factor: 3.162

7.  Interactions of aminoacyl-tRNA synthetases in high-molecular-weight multienzyme complexes from rat liver.

Authors:  C V Dang; B Ferguson; D J Burke; V Garcia; D C Yang
Journal:  Biochim Biophys Acta       Date:  1985-07-01

8.  Seven mammalian aminoacyl-tRNA synthetases associated within the same complex are functionally independent.

Authors:  M Mirande; B Cirakoğlu; J P Waller
Journal:  Eur J Biochem       Date:  1983-03-01

9.  Molecular weights of mitochondrial and cytoplasmic aminoacyl-tRNA synthetases of beef liver and their complexes.

Authors:  E J Walker; G B Treacy; P D Jeffrey
Journal:  Biochemistry       Date:  1983-04-12       Impact factor: 3.162

10.  Macromolecular complexes of aminoacyl-tRNA synthetases from eukaryotes. 1. Extensive purification and characterization of the high-molecular-weight complex(es) of seven aminoacyl-tRNA synthetases from sheep liver.

Authors:  O Kellermann; A Brevet; H Tonetti; J P Waller
Journal:  Eur J Biochem       Date:  1979-09
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