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Biomedical subjects

Z Yuan

Publications and source records attributed to Z Yuan.

166 records · Page 10Linked to original sources
PubMed1985

Immediate converting-enzyme inhibition with intravenous enalapril in chronic congestive heart failure.

To test the hypothesis that intravenous enalapril is a useful pharmacologic probe of the renin angiotensin system, intravenous enalapril was administered to 9 patients with severe congestive heart failure (CHF). This produced abrupt and complete blockade of converting enzyme, with peak effect occurring at 30 minutes, as reflected by increases of plasma renin activity (from 16.8 +/- 6 to 86.6 +/- 23 ng/ml/hour) and decreases of plasma aldosterone levels (from 46 +/- 14 to 25 +/- 6 ng%) (both p less than 0.05). With reduction of angiotensin II--mediated vasoconstriction, systemic vascular resistance decreased markedly (from 1,974 +/- 233 to 1,400 +/- 136 dyne s cm-5) and cardiac index was improved (from 1.88 +/- 0.9 to 2.20 +/- 0.21 liters/min/m2) (both p less than 0.05). The time course of angiotensin II levels suggested that the lack of a cumulative effect from additive doses of intravenous enalapril was a reflection of complete inhibition of converting enzyme. One patient did not respond to enalapril; despite comparable hemodynamic severity of CHF, the renin-angiotensin system was not activated in this patient. Thus, intravenous enalapril is capable of rapid and complete inhibition of converting enzyme for the accurate assessment of angiotensin II--mediated vasoconstriction in patients with severe CHF.

Adult↗
PubMed1984

Elementary steps in the reaction mechanism of chicken liver fatty acid synthase. pH dependence of NADPH binding and isotope rate effect for beta-ketoacyl reductase.

The stopped flow method has been used to determine the pH dependence of the kinetics of the binding of NADPH to chicken liver fatty acid synthase over the pH range 6.0-8.5. The kinetics is consistent with a one-step binding mechanism, and the pH dependence of the second order rate constant indicates that an ionizable group either on the enzyme or on NADPH with a pK alpha of 6.1 is of importance in the binding process. The isotope rate effects have been determined for the steady state reaction with (S)- and (R)-[4-2H] NADPH as substrates and are very small. The pH dependence of the rate constant characterizing the reduction of acetoacetyl by NADPH on the enzyme (beta-ketoacyl reductase) and the isotope rate effects on this constant with (S)-[4-2H]NADPH as substrate also have been measured with the stopped flow method. A small pH-dependent isotope rate effect is found; these results suggest hydride transfer is not rate limiting for the beta-ketoacyl reductase reaction on the enzyme surface. The pH dependence of this rate constant is bell shaped and is very similar to that of the turnover number for the overall reaction; this suggests that the beta-ketoacyl reductase reaction may be partially rate limiting for the overall reaction when the enzyme is saturated with substrates.

Alcohol Oxidoreductases↗