Abstract:
:Polypeptides rich in glutamic acid are strong inhibitors purified from isolated nuclei of Xenopus laevis oocytes of casein kinase II. The presence of tyrosine in these peptides greatly enhances their inhibitory capacity. Using casein as a substrate, copolyglu:tyr (4:1) has an I50 value of 20 nM, 250 fold lower than that of polyglutamic acid which is 5 microM. A similar large difference is observed when a synthetic peptide is used as substrate. The inhibition of copolyglu:tyr is competitive with casein and can be completely reversed by high ionic strength. The relative inhibitory capacity of the polypeptides tested, in descending order, is copolyglu:tyr (4:1) greater than copolyglu:tyr (1:1) greater than polyglu greater than copolyglu:phe (4:1) greater than copolyglu:ala (6:4) greater than copolyglu:leu (4:1). The high affinity for tyrosine-containing acid peptides is shared by rat liver and yeast casein kinase II so that it seems to be a general property of these enzymes.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Tellez R,Gatica M,Allende CC,Allende JEdoi
10.1016/0014-5793(90)80897-rsubject
Has Abstractpub_date
1990-06-04 00:00:00pages
113-6issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(90)80897-Rjournal_volume
265pub_type
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