Exploration of insecticidal potential of an alpha glucosidase enzyme inhibitor from an endophytic Exophiala spinifera

2018 ◽  
Vol 125 (5) ◽  
pp. 1455-1465 ◽  
Author(s):  
J. Kaur ◽  
R. Kaur ◽  
R. Datta ◽  
S. Kaur ◽  
A. Kaur
Keyword(s):  
Enzyme Inhibitor ◽  
Exophiala Spinifera ◽  
Alpha Glucosidase

Butea Frondosa, A Rho Kinase 2 and Phosphodiesterase 5 Enzyme Inhibitor, Increases Sexual Function In Young And Aged Rats

Planta Medica ◽  
2013 ◽  
Vol 79 (10) ◽  
Author(s):  
S Kumar Goswami ◽  
M Naseeruddin Inamdar ◽  
S Dethe ◽  
A Agarwal
Keyword(s):  
Sexual Function ◽  
Enzyme Inhibitor ◽  
Rho Kinase ◽  
Aged Rats ◽  
Phosphodiesterase 5

Thrombospondin 1 as an Enzyme Inhibitor

1994 ◽  
Vol 72 (06) ◽  
pp. 787-792 ◽  
Author(s):  
Philip J Hogg
Keyword(s):  
Enzyme Inhibitor ◽  
Thrombospondin 1

Fast and Reproducible Vascular Neointima Formation in the Hamster Carotid Artery: Effects of Trapidil and Captopril

1995 ◽  
Vol 74 (06) ◽  
pp. 1591-1596 ◽  
Author(s):  
H Matsuno ◽  
J M Stassen ◽  
M F Hoylaerts ◽  
J Vermylen ◽  
H Deckmyn
Keyword(s):  
Carotid Artery ◽  
Enzyme Inhibitor ◽  
Neointima Formation ◽  
Proliferating Cells ◽  
Dental Cement ◽  
Proliferation Indices ◽  
Experimental Drugs ◽  
The Media ◽  
Von Willebrand ◽  
Willebrand Factor

SummaryNeointima formation was induced in the hamster carotid artery by mechanical intraluminal injury with a catheter covered with roughened dental cement. Neointimal thickening occurred as early as 7 days after denudation and further increased during the next 1 to 2 weeks. Proliferation indices of smooth muscle cells (SMCs) showed the highest proportion of proliferating cells in the media and neointima respectively 1 and 5 days after the vascular injury. Transmission and scanning electron microscopy of damaged carotid artery sections as well as immuno-histochemical stainings of von Willebrand factor (vWF) confirmed that reendothelialization was progressive and already complete on day 14, at which time the neointima formation was almost complete.In order to pharmacologically characterize this model further, the effects on neointima formation of trapidil (triazolopyrimidine), a platelet-derived growth factor (PDGF) antagonist, and captopril, an angiotensin converting enzyme inhibitor, were investigated. Trapidil administered orally twice daily at total doses of 25, 50 and 100 mg/kg/day, started 3 days prior to infliction of injury and up to 7 or 14 days after the catheterization, significantly reduced neointima formation. Captopril administered orally three times daily at a total dose of 100 mg/kg/day, equally reduced neointima formation, with 100 mg/kg/day trapidil being more effective than 100 mg/kg/day captopril 7 days after injury. When the treatment by either one of these drugs was arrested on day 7, neointima formation resumed quickly.The hamster appears to be a small, reproducible and fast model for the study of SMC proliferation, requiring only relatively small amounts of experimental drugs. The model furthermore is sensitive to substances known to reduce neointima formation in other animal models.

Preparation and Properties of Human Prothrombin Complex

1970 ◽  
Vol 24 (03/04) ◽  
pp. 325-333 ◽  
Author(s):  
G. H Tishkoff ◽  
L. C Williams ◽  
D. M Brown
Keyword(s):  
Molecular Weight ◽  
Proteolytic Enzyme ◽  
Enzyme Inhibitor ◽  
Specific Activity ◽  
Crystalline Form ◽  
Sedimentation Equilibrium ◽  
Crystalline Complex ◽  
Interaction Product ◽  
Proteolytic Enzyme Inhibitor ◽  
Purification Scheme

SummaryAs a corollary to our previous studies with bovine prothrombin, we have initiated a study of human prothrombin complex. This product has been isolated in crystalline form as a barium glycoprotein interaction product. Product yields were reduced compared to bovine product due to the increased solubility of the barium glycoprotein interaction product. On occasion the crystalline complex exhibited good yields. The specific activity of the crystalline complex was 1851 Iowa u/mg. Further purification of human prothrombin complex was made by removal of barium and by chromatography on Sephadex G-100 gels. The final product evidenced multiple procoagulant activities (II, VII, IX and X). The monomeric molecular weight determined by sedimentation equilibrium in a solvent of 6 M guanidine-HCl and 0.5% mercaptoethanol was 70,191 ± 3,057 and was homogeneous with respect to molecular weight. This product was characterized in regard to physical constants and chemical composition. In general, the molecular properties of human prothrombin complex are very similar to the comparable bovine product. In some preparations a reversible proteolytic enzyme inhibitor (p-aminophenylarsonic acid) was employed in the ultrafiltration step of the purification scheme to inhibit protein degradation.

m-[o-(2-Chloro-5-Fluorosulfonylphenylureido)Phenoxybutoxy]Benzamidine: Affinity Labeling Reagent Which Can Identify Secondary Binding Sites of Coagulation Complement and Fibrinolytic Serine Proteases

1979 ◽  
Author(s):  
D Bing ◽  
D Robison ◽  
J Andrews ◽  
R Laura
Keyword(s):  
Binding Sites ◽  
Serine Proteases ◽  
Enzyme Inhibitor ◽  
Molecular Model ◽  
Factor Xa ◽  
Affinity Labeling ◽  
Catalytic Center ◽  
Inhibitor Complex ◽  
Polypeptide Chains ◽  
Kinetics Of

We have determined that m-[o-(2-chloro-5-fluorosulfonylphenylureido)phenoxybutoxy]benza-midine [mCP(PBA)-F] is an affinity labeling reagent which labels both polypeptide chains of thrombin, factor Xa, complement component CIS and plasmin. As this means it is reacting outside of the catalytic center, we have called this reagent an exo-site affinity labeling reagent. Progressive irreversible inhibition of these enzymes by this reagent is rapid (k1st 2.5-4.6 x 10-3sec-1), the kinetics of inactivation are consistent with inhibition proceding via formation of a specific enzyme-inhibitor complex analogous to a Michaelis-Menton complex (KL - 115-26 μM), and diisopropylfluorophosphate or p-amidino-phenylmethanesulfonyfluoride Prevent labeling by [3H]mCP(PBA)-F. A molecular model of mCP(PBA)-F shows that the reactive SO2F group can be 17 A from the cationic amidine. The data are consistent with the hypothesis that both peptide chains are required for the specific proteolytic activity exhibited by these proteases and that the peptide chain which does not contain the active site serine is close to the catalytic center. (Supported by NIH and AHA grants

Fixed combination in patients with arterial hypertension: focus on antihypertensive and nephroprotective properties of fixed combination of lisinopril and amlodipine (clinical example)

2020 ◽  
pp. 19-28
Author(s):  
E. Yu. Ebzeeva ◽  
O. D. Ostroumova ◽  
N. M. Doldo ◽  
E. E. Pavleeva
Keyword(s):  
Kidney Disease ◽  
Arterial Hypertension ◽  
Fixed Combination ◽  
Enzyme Inhibitor ◽  
Antihypertensive Drugs ◽  
Adult Population ◽  
Secondary Damage ◽  
Dihydropyridine Calcium Channel Blocker ◽  
Based Medicine ◽  
Modern Population

Arterial hypertension (AH) remains one of the most significant medical and social problems in the world, its prevalence among the adult population is 30–45%. Along with this, the modern population is characterized by a high incidence of chronic kidney disease (CKD), including due to their secondary damage in the framework of hypertension. In turn, CKD is an important independent risk factor for the development and progression of cardiovascular diseases, including fatal ones. The use of existing approaches to nephroprotection in the treatment of patients with hypertension will significantly improve the prognosis both in patients with risk factors for developing renal dysfunction and in patients with pre-existing kidney disease. According to current recommendations for hypertension in such clinical situations, therapy should begin with fixed combinations of antihypertensive drugs. The combination of an angiotensin converting enzyme inhibitor (ACE) and a dihydropyridine calcium channel blocker (CCВ) demonstrated the greatest effectiveness according to evidence-based medicine in patients with high-risk hypertension, including from the standpoint of nephroprotection. In the presented clinical case, the successful use of a fixed combination of ACE and CCВ in a patient with hypertension and microalbuminuria is described.

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