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The ribonuclease inhibitors from porcine thyroid and liver are slow, tight-binding inhibitors of bovine pancreatic ribonuclease A.

Abstract：

:Ribonuclease inhibitors were purified from the latent ribonuclease fractions of porcine thyroid and liver and used to test the hypothesis that their inhibition of bovine pancreatic ribonuclease A is correctly described by tight-binding rather than Michaelis-Menton kinetics. Both proteins were found to act as slow, tight-binding inhibitors of the enzyme. These steady-state velocities also showed that both the thyroid and liver inhibitors were competitive inhibitors of bovine pancreatic ribonuclease A with Ki's of 0.1 and 0.4 nM, respectively. In contrast to interpretations based on Michaelis-Menton assumptions that show non-competitive inhibition, these results suggest that an enzyme:inhibitor:substrate complex does not exist.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Turner PM,Lerea KM,Kull FJ

doi

10.1016/0006-291x(83)90683-6

subject

Has Abstract

pub_date

1983-08-12 00:00:00

pages

1154-60

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(83)90683-6

journal_volume

114

pub_type

杂志文章

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