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.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Berbeć H,Paszkowska Adoi
10.1007/BF00222612subject
Has Abstractpub_date
1989-04-11 00:00:00pages
125-33issue
2eissn
0300-8177issn
1573-4919journal_volume
86pub_type
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journal_title:Molecular and cellular biochemistry
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journal_title:Molecular and cellular biochemistry
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journal_title:Molecular and cellular biochemistry
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journal_title:Molecular and cellular biochemistry
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journal_title:Molecular and cellular biochemistry
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