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H Berbeć

Publications and source records attributed to H Berbeć.

16 recordsLinked to original sources
PubMed1994

[Human gene p53].

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Amino Acid Sequence↗
PubMed1993

[High molecular weight forms of aminoacyl-tRNA synthetases in animals. I. Amount and enzymatic composition of high molecular weight synthetase in cytosol from rabbit liver].

A high-molecular-weight complex composed of 15 amino acid-tRNA synthetases occurs in the rabbit liver cytosol apart from the free enzymes. The greatest activities in the complex are exhibited by lysyl- and arginyl-tRNA synthetases. The complex has the mass of about 4,000 kDa and the sedimentation constant about 19 S.

Amino Acyl-tRNA Synthetases↗
PubMed1993

[High molecular weight forms of aminoacyl-tRNA synthetases in animals. II. High molecular weight aminoacyl-tRNA synthetase complexes in lower animals].

High-molecular-weight aminoacyl-tRNA synthetase complexes have been found in hen, frog and carp liver cytosol as well as in cytosol from snails and Paramecium. The complexes from vertebrates and snails contained 13-15 aminoacyl-tRNA synthetases, revealed mass of about 4,000 kDa and sedimentation constant about 19 S. The complex from Paramecium containing 11 aminoacyl-tRNA synthetases, revealed a mass of about 1,600 kDa and sedimentation constant 15 S. The results of the present study support the view that the high-molecular-weight synthetase complexes are common entities in the animal kingdom.

Amino Acyl-tRNA Synthetases↗
PubMed1989

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

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.

Amino Acyl-tRNA Synthetases↗
PubMed1984

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

Aminoacyl-tRNA synthetase activity for alanine, glutamic acid, lysine and phenylalanine was studied in the three subcellular fractions of rabbit liver: fraction X, microsomes and cytosol. From 60 to 80% of the enzyme activities were found in fraction X and microsomes. Fraction X was especially rich in the synthetase activities. By means of gel chromatography, heavy (over 10(6) daltons) and light (below 480 X 10(3) daltons) forms of lysyl- and phenylalanyl- but only light ones of alanyl- and glutamyl-tRNA synthetase activities were found in all the subcellular fractions studied. It is concluded that in higher organisms (mammals) all aminoacyl-tRNA synthetases, at least in part, are associated with cell structural constituents.

Amino Acyl-tRNA Synthetases↗