Protamine Kinase from Rainbow Trout Testis PARTIAL PURIFICATION AND CHARACTERIZATION
作者： Bengt Jergil , Gordon H. Dixon
DOI: 10.1016/S0021-9258(18)63408-8
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摘要: Abstract A Mg2+-dependent enzyme which will phosphorylate protamines and histones has been isolated purified approximately 30-fold from rainbow trout testis. The transfers the terminal phosphoryl group ATP (but not cytidine, guanosine, or uridine triphosphates) into O-phosphoseryl linkages in acceptor molecule. is dependent on addition of thiol compounds for maximal activity cyclic 3',5'-AMP stimulates both protamine histone phosphorylation. At a high ionic strength (0.3 m NaCl), rate phosphorylation enhanced 3-fold while suppressed. KCl, ammonium chloride, sodium acetate have same effect as NaCl. Mg2+ essential can also satisfy requirement activity. In low medium slightly higher than that unfractionated histones, but presence 0.3 NaCl ratio to rises 13.5. Of different fractions, lysine-rich fraction most readily phosphorylated by arginine-rich fractions are poor substrates. Casein free serine small extent. Enzymatically be separated unphosphorylated starch gel electrophoresis.
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