Abstract:
:The rate at which dinucleoside phosphates are cleaved by RNases is supposed to be determined by the mole fraction of enzyme-substrate complexes in which the phosphodiester moiety of a dinucleoside phosphate has a highly reactive conformation. The mole fraction of such complexes for a particular RNase depends on the nature of a nucleoside at the O5'-end of the phosphodiester bond. Experimental data are presented to support this hypothesis.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Yakovlev GI,Bocharov AL,Moiseyev GP,Mikhaylov SNdoi
10.1016/0014-5793(85)80521-4subject
Has Abstractpub_date
1985-01-07 00:00:00pages
217-20issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(85)80521-4journal_volume
179pub_type
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