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  • 1
    Online Resource
    Online Resource
    Get Your Ass in the Water and Swim Like Me : African-American Narrative Poetry from the Oral Tradition, Includes CD (2004)
    London : Routledge
    Details Availability
    Keywords: Toasts (African American folk poetry) ; Toasts (African American folk poetry) ; Electronic books
    Description / Table of Contents: First published in 2004. Routledge is an imprint of Taylor & Francis, an informa company.
    Type of Medium: Online Resource
    Pages: 1 online resource (243 pages)
    Edition: 1st ed.
    ISBN: 9780203323311
    URL: https://ebookcentral.proquest.com/lib/kxp/detail.action?docID=199671
    DDC: 811.008
    Language: English
    Note: Description based on publisher supplied metadata and other sources
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  • 2
    Electronic Resource
    Electronic Resource
    Direct heated interface probe for capillary supercritical fluid chromatography/double focusing mass spectrometry (1988)
    s.l. : American Chemical Society
    Analytical chemistry 60 (1988), S. 2715-2719 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac00175a015
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  • 3
    Electronic Resource
    Electronic Resource
    MESENTERIC VASCULAR ANGIOTENSIN-CONVERTING ENZYME IS INCREASED IN EXPERIMENTAL DIABETES MELLITUS (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 19 (1992), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. Diabetes mellitus was induced by streptozotocin in male Wistar rats, and angiotensin-converting enzyme measured in plasma and mesenteric vessels 3 weeks later.2. Diabetes was associated with increased mesenteric wet weight/ bodyweight ratio (control 0.2 s.e.m. 0.02 mg/g, n= 21, vs diabetes 1.0 s.e.m. 0.3 mg/g, n= 27, P 〈 0.01, ANOVA).3. Plasma angiotensin-converting enzyme activity was increased in diabetic rats (98 s.e.m. 3 nmol HL/mL per min) compared with controls (64 s.e.m. 6 nmol HL/mL per min, P 〈 0.01, ANOVA).4. Mesenteric vessel angiotensin-converting enzyme was increased in diabetes mellitus estimated by radioligand binding site density (fmol/mg protein; 1407 s.e.m. 166 fmol/mg protein) compared with controls (890 s.e.m. 56 fmol/mg protein, P 〈 0.05, ANOVA) and by enzyme kinetic assay (diabetes, 15.5 s.e.m. 1.5 nmol HL/mg protein per min, controls, 8.3 s.e.m. 0.7 nmol HL/mg protein per min, P 〈 0.01, ANOVA). The equilibrium dissociation constant of ligand-angiotensin-converting enzyme interaction was unchanged.5. Increased vascular angiotensin-converting enzyme concentration may contribute to vascular hypertrophy and diabetic vasculopathy by increased local synthesis of angiotensin II.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1992.tb00468.x
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  • 4
    Electronic Resource
    Electronic Resource
    VARIATION IN ANGIOTENSIN-CONVERTING ENZYME (ACE) INHIBITOR AFFINITY AT TWO BINDING SITES ON RAT PULMONARY ACE: INFLUENCE ON BRADYKININ HYDROLYSIS (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 19 (1992), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. ACE from rat lung and testis was characterized by radioligand binding studies using [125I]-Ro 31-8472, the radioiodinated hydroxy derivative of the potent ACE inhibitor cilazaprilat.2. Analysis of the displacement of [125I]-Ro 31-8472 from ACE by ACE inhibitors of different structure by the ligand program was best fitted by a two binding site model for lung ACE and a one binding site model for testis ACE.3. There was marked variation in ACE inhibitor binding affinity at the two binding sites of lung ACE across the panel of ACE inhibitors studied (equilibrium dissociation constant; Kd; pmol/ L) for site one vs site two: cilazaprilat 40 ± 3 vs 430 ± 92*; lisinopril 25±1 vs 848 ± 107**; and quinaprilat 4 ± 1 vs 1869 ± 720; **P 〈 0.05; **P 〈 0.005, t-test, n= 3). Reduction in binding affinity at site two of lung ACE was related to an increase in ACE inhibitor side chain length or complexity of carboxyl terminal moiety. ACE inhibitor binding affinity at the testis ACE binding site resembled site one of lung ACE.4. Inhibition of bradykinin hydrolysis by lung ACE in the presence of increasing concentrations of cilazaprilat or quinaprilat was similar (F= 0.64; P〉0.05), suggesting that bradykinin cleavage predominates at ACE active site one.5. The differences in ACE inhibitor affinity at the two ACE active sites has implications in physiological substrate selectivity, and may influence the pharmacodynamic effects of different ACE inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1992.tb00470.x
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  • 5
    Electronic Resource
    Electronic Resource
    BLOCKADE OF ANGIOTENSIN CONVERTING ENZYME IN CIRCUMVENTRICULAR ORGANS OF THE BRAIN AFTER ORAL LISINOPRIL ADMINISTRATION DEMONSTRATED BY QUANTITATIVE IN VITRO AUTORADIOGRAPHY (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 14 (1987), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. To elucidate the central effect of lisinopril, a new angiotensin converting enzyme (ACE) inhibitor, ACE localization and levels were followed in the brain of Sprague-Dawley rats by quantitative in vitro autoradiography after administration of the drug.2. Following acute lisinopril (10 mg/kg p.o.) treatment, serum ACE activity was acutely reduced, but returned to normal by 24 h.3. Levels of ACE in most parts of the brain, including the basal ganglia and choroid plexus of all ventricles were not affected by lisinopril. Lisinopril inhibited brain ACE in the subfornical organ and organum vasculosum of the lamina terminalis, circumventricular organs, where the blood brain barrier is deficient. These regions are rich in ACE and angiotensin II receptors, and are known targets for angiotensin II-induced effects on fluid, electrolyte and blood pressure homeostasis.4. These observations indicate that quantitative in vitro autoradiography is a powerful method to study the access of drugs to the central nervous system.5. This study shows that blood brain barrier plays an important role in limiting the penetration of lisinopril into the central nervous system. The circumventricular organs may be important targets for ACE inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1987.tb00367.x
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  • 6
    Electronic Resource
    Electronic Resource
    HIGH SALT DIET AMELIORATES EFFECTS OF ANGIOTENSIN CONVERTING ENZYME INHIBITION IN SPONTANEOUSLY HYPERTENSIVE STREPTOZOTOCIN DIABETIC RATS (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 17 (1990), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. To dissociate the effects on the development of diabetic renal injury of angiotensin converting enzyme (ACE) inhibition per se, and a reduction in systemic blood pressure, we have studied the effects of chronic ramapril treatment in streptozotocin diabetic spontaneously hypertensive rats, with modulation of the hypotensive effect by a high salt diet.2. Three weeks following uninephrectomy and induction of diabetes with streptozotocin, spontaneously hypertensive rats were allocated to three treatment groups. Groups 1 and 2 received 1% sodium chloride and Group 3 water as drinking solution. Groups 2 and 3 received 0.4 mg/kg per day ramapril in drinking solution over the subsequent 2 month study period.3. Sodium chloride drinking solution (1%) completely prevented any hypotensive effect of ramapril. Blood pressure was reduced in Group 3 rats over the entire period of study, when compared with Group 2 rats (P〈0.001).4. Urinary protein excretion progressively increased in Group 1 and 2 rats, and was significantly reduced (P〈0.001) in Group 3. After 2 months treatment, urinary protein (expressed as mean and s.e.m.) was 160±30 mg/day in Group 1, 240±50 mg/day in Group 2, and 60±11 mg/day in Group 3.5. Angiotensin converting enzyme inhibition per se was not associated with a reduced protein excretion in diabetic nephropathy, requiring concomitant control of systemic blood pressure to become renoprotective.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1990.tb01312.x
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  • 7
    Electronic Resource
    Electronic Resource
    PLASMA ATRIAL NATRIURETIC PEPTIDE: CONCENTRATIONS AND CIRCULATING FORMS IN NORMAL MAN AND PATIENTS WITH CHRONIC RENAL FAILURE (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 14 (1987), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: SUMMARY1. A specific and sensitive radioimmunoassay has been developed and used to measure circulating atrial natriuretic peptide (ANP) in normal man and in patients with chronic renal failure.2. Circulating ANP levels rose with head-down tilt and exercise, and were raised in patients with chronic renal failure in proportion to volume status. This suggests that ANP release is mediated via increased atrial stretch, although other release mechanisms cannot be excluded.3. Extracts of normal human plasma subjected to reverse phase HPLC showed one major peak of immunoreactivity co-migrating with α-human ANP. However, when plasma extracts from patients with renal failure were chromatographed on a similar system, a second later eluting peak of ANP immunoreactivity was observed. This may represent circulating ANP precursors or degradation molecules.4. Significant arteriovenous differences in plasma ANP concentration were observed in patients with chronic renal failure. Arterial and venous plasma ANP levels decreased slightly after haemodialysis. Plasma ANP concentrations were inversely correlated with haematocrit in these patients.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1987.tb00962.x
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  • 8
    Electronic Resource
    Electronic Resource
    ACUTE AND CHRONIC EFFECTS OF ANGIOTENSIN-CONVERTING ENZYME INHIBITORS ON TISSUE ANGIOTENSIN-CONVERTING ENZYME (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 19 (1992), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. The effects of angiotensin-converting enzyme (ACE) inhibitors on the tissue ACE were assessed by quantitative in vitro autoradiography after acute and chronic administrations of the drugs.2. Following acute administration of lisinopril, perindopril or benazepril, ACE was markedly inhibited in the lung, kidney and blood vessels but not in the testis. In the brain, ACE was inhibited mainly in structures with a deficient blood brain barrier.3. High doses of perindopril progressively inhibited ACE in other brain structures. Tissue ACE inhibition persisted after serum levels of the enzyme had returned to control levels. In the case of perindopril, the time course of tissue ACE inhibition correlated with the inhibition of the pressor responses to exogenous angiotensin I.4. After chronic administration of lisinopril or perindopril for 14 days, a similar pattern of ACE inhibition was observed in the kidney, lung and blood vessels. In the lung, however, lisinopril was found to increase total ACE by 30%, while plasma ACE was increased two-threefold by both lisinopril and perindopril. Testicular ACE remained unaltered by chronic lisinopril treatment.5. Overall, the changes in tissue ACE after the administration of inhibitors more closely parallel the drugs' biological effects than changes in plasma ACE or drug levels. ACE in the testis and brain is protected by permeability barriers that limit access of the drugs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1992.tb02803.x
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  • 9
    Electronic Resource
    Electronic Resource
    CHARACTERIZATION OF ANGIOTENSIN CONVERTING ENZYME FROM RAT TISSUE BY RADIO-INHIBITOR BINDING STUDIES (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 13 (1986), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. Angiotensin converting enzyme (ACE) derived from rat lung, aorta, epididymus, brain, kidney and plasma was characterized by radio-inhibitor (125I-MK351A) binding studies. Under optimal binding conditions at equilibrium 125I-MK351A bound to ACE was displaced from ACE in a concentration related manner by unlabelled MK351A.2. MK351A binding site concentration for each tissue and equilibrium dissociation constant (KD) was estimated by Scatchard analysis of binding data. Binding sites/mg protein was greatest in lung and least in brain. The KD for kidney ACE was significantly higher than that of lung, aorta, epididymus or brain ACE (P〈0.005; t-test, d.f. = 10).3. 125I-MK351A bound to ACE prepared from lung and kidney was displaced in a concentration dependent manner by SQ20881, SQ14225, MK422, and Ro31–3113–000. Concentration of ACE inhibitor required to displace 50% of bound 125I-MK351A (DD50) was consistently higher for kidney-derived ACE than lung-derived ACE.4. The differences in radio-inhibitor binding characteristics of ACE from different rat tissues suggests that the enzyme active site may not be identical in all organs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1986.tb02397.x
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  • 10
    Electronic Resource
    Electronic Resource
    GENOTYPIC INFLUENCE ON PLASMA DIPEPTIDYL CARBOXYPEPTIDASE-1 ACTIVITY IN HYPERTENSIVES (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 21 (1994), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. Plasma dipeptidyl carboxypeptidase-1 (DCP1; angiotensin I-converting enzyme, kininase II; EC 3.4.15.1) tracks with the deletion allele in genotypes of a 287 bp insertion/deletion (I/D) polymorphism of its gene, DCP1, in healthy Caucasian populations. The aim of the present study was to see whether genotype has a similar influence on plasma DCP1 in hypertensives.2. The study involved 35 Caucasian patients with severe, familial essential hypertension, who were not being treated with DCP1 inhibitors, and 94 normotensives. Genotyping for the I/D polymorphism was performed by polymerase chain reaction and plasma DCP1 activity was measured by rate of hydrolysis of both [3H]-Hip-Gly-Gly and Hip-His-Leu.3. Plasma DCP1 activity (nmol Gly-Gly/min per mL; mean ± s.e.m.) was 67 ± 2, 82 ± 4 and 91 ± 6 in II, ID and DD hypertensives, respectively, which was similar to values of 68 ± 4, 82 ± 3 and 94 ± 3 in normotensives (P= 0.0001 by one-way analysis of variance). Results for the His-Leu assay indicated similar tracking with genotype.4. The Michaelis constant (μmol Hip-Gly-Gly/mL; mean ± s.e.m., n= 10) for DD subjects was the same as for II subjects (10.6 ± 1.6 vs 11.1 ± 2.3; P = 0.86).5. In conclusion, in severely hypertensive Caucasian subjects, plasma DCP1 activity is subject to a similar genotypic influence in hypertensives as has been reported previously in normotensives. Furthermore, the plasma DCP1 enzyme itself appears to be functionally similar for each genotype.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1994.tb02525.x
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