Time-Dependent Inactivation of Aromatase by 6-Alkylandrosta-1,4-diene-3,17-diones. Effects of Length and Configuration of the 6-Alkyl Group†

1996 ◽  
Vol 39 (5) ◽  
pp. 1033-1038 ◽  
Author(s):  
Mitsuteru Numazawa ◽  
Mariko Oshibe ◽  
Satoshi Yamaguchi ◽  
Mii Tachibana
Keyword(s):  
Alkyl Group ◽  
Time Dependent ◽  
Dependent Inactivation

Differential Time-Dependent Inactivation of P450 3A4 and P450 3A5 by Raloxifene: A Key Role for C239 in Quenching Reactive Intermediates

2007 ◽  
Vol 20 (12) ◽  
pp. 1778-1786 ◽  
Author(s):  
Josh T. Pearson ◽  
Jan L. Wahlstrom ◽  
Leslie J. Dickmann ◽  
Santosh Kumar ◽  
James R. Halpert ◽  
...  
Keyword(s):  
Reactive Intermediates ◽  
Time Dependent ◽  
Dependent Inactivation

Time-dependent inactivation of steroid C17(20) lyase by 17β-cyclopropyl ether-substituted steroids

1996 ◽  
Vol 6 (1) ◽  
pp. 97-100 ◽  
Author(s):  
Michael R. Angelastro ◽  
Angela L. Marquart ◽  
Philip M. Weintraub ◽  
Cynthia A. Gates ◽  
Marie E. Laughlin ◽  
...  
Keyword(s):  
Time Dependent ◽  
Dependent Inactivation

scholarly journals Rhodopsin kinase: Two mAbs binding near the carboxyl terminus cause time-dependent inactivation

2000 ◽  
Vol 97 (7) ◽  
pp. 3010-3015 ◽  
Author(s):  
C. Bruel ◽  
K. Cha ◽  
L. Niu ◽  
P. J. Reeves ◽  
H. G. Khorana
Keyword(s):  
Time Dependent ◽  
Carboxyl Terminus ◽  
Dependent Inactivation ◽  
Rhodopsin Kinase

EVALUATION OF TIME-DEPENDENT INACTIVATION OF CYP3A IN CRYOPRESERVED HUMAN HEPATOCYTES

2005 ◽  
Vol 33 (6) ◽  
pp. 853-861 ◽  
Author(s):  
Ping Zhao ◽  
Kent L. Kunze ◽  
Caroline A. Lee
Keyword(s):  
Human Hepatocytes ◽  
Time Dependent ◽  
Dependent Inactivation

Glucose-6-phosphatase: is activity regulated by phosphorylation–dephosphorylation?

1983 ◽  
Vol 61 (10) ◽  
pp. 1085-1089 ◽  
Author(s):  
Jasbir Singh ◽  
Richard E. Martin ◽  
Robert C. Nordlie
Keyword(s):  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Alternative Explanation ◽  
Potent Inhibitor ◽  
Liver Microsomes ◽  
Time Dependent ◽  
Rat Liver Microsomes ◽  
Phosphoprotein Phosphatase ◽  
Dependent Inactivation ◽  
Competitive Inhibitors

Incubation of rat liver microsomes with ATP and Mg2+ in the absence or presence of an exogenous protein kinase showed no changes in the activity of glucose-6-phosphatase (D-glucose-6-phosphate phosphohydrolase, EC 3.1.3.9). These observations confirm the recent findings of the Burchells and colleagues and refute on methodological grounds the earlier conclusions of Begley and Craft implicating regulation of this enzyme by protein phosphorylation–dephosphorylation. In other studies, the time-dependent inactivation of microsomal glucose-6-phosphatase by incubation with deoxycholate was used to obtain the inactive enzyme which in the presence of a protein kinase, ATP, and Mg2+ could not be restored to its original level. A number of substrates and competitive inhibitors of glucose-6-phosphatase, most notably vanadate which is the most potent inhibitor of the enzyme identified, stabilized this enzyme against its time-dependent inactivation in the presence of detergent as effectively as did fluoride and molybdate which are also effective competitive inhibitors of glucose-6-phosphatase. An alternative explanation to the involvement of a phosphoprotein phosphatase, as discussed by the Burchells, in the time-dependent inactivation of glucose-6-phosphatase is thus suggested.

Effect of external Ca2+ concentration on stretch-augmented natriuretic peptide secretion by rat atria

1991 ◽  
Vol 260 (4) ◽  
pp. C756-C762 ◽  
Author(s):  
E. Page ◽  
J. Upshaw-Earley ◽  
G. E. Goings ◽  
D. A. Hanck
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Natriuretic Peptide ◽  
Time Course ◽  
Rate Coefficient ◽  
Time Dependent ◽  
Dependent Manner ◽  
Dependent Inactivation ◽  
Long Time ◽  
Peptide Secretion

An in vitro noncontracting rat atrial preparation stretched at 37 degrees C by a distending pressure of 5.1 mmHg was used to examine effects of external Ca2+ concentration ([Ca2+]out, 0.05-3.0 mM) on secretion of immunoreactive atrial natriuretic peptide (ANP) in presence of saxitoxin (STX) and in presence or absence of ryanodine. Under these conditions, the time course of the amount (y) of ANP secreted per milligram dry atrium during 44 min could be approximated by a rate coefficient (k) according to the relation y = s[1 - e(-kt)], where s is the maximal amount secreted after a long time (t). Although k, the rate coefficient for stretch-augmented secretion, increased significantly as [Ca2+]out was raised, secretion inactivated progressively in a time- and [Ca2+]out-dependent manner. This time-dependent decrease was not prevented by ryanodine. We conclude that a component of ANP secreted by quiescent atria in vitro is positively modulated by [Ca2+]out and does not require ryanodine-sensitive Ca2+ release from sarcoplasmic reticulum. The [Ca2+]out-sensitive processes underlying time-dependent inactivation of secretion remain undetermined.

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