A Phase 1b, Double-Blind, Placebo-Controlled, First-in-Human Study to Evaluate Safety, Tolerability and Pharmacokinetics of a Two-Week Oral Treatment With STP1 in a Subgroup of Patients With Autism Spectrum Disorder

The main purpose of this study is to evaluate safety and tolerability, Pharmacokinetics and Pharmacodynamics, as well as exploratory efficacy of STP1, in a subgroup of patients with Autism Spectrum Disorder (ASD).

Start Date07 Dec 2020

Sponsor / Collaborator

Stalicla SAStartup

NCT00102050 / CompletedPhase 2

A Double-Blind, Randomized, Parallel Group, Placebo-Controlled Study to Evaluate the Safety and Efficacy of NM-702 in Subjects With Intermittent Claudication

NM-702 oral tablets are being developed for the treatment of Intermittent Claudication, a primary early stage indication of peripheral arterial disease (PAD). This trial is designed to assess the safety and efficacy of 4 mg and/or 8 mg NM-702 taken twice a day (BID) for 24 weeks to see if it improves peak walking time (PWT) more than placebo for the treatment of Intermittent Claudication.

Start Date01 Apr 2003

Sponsor / Collaborator

Nissan Chemical Corp.

100 Clinical Results associated with Phosphoric diester hydrolases

100 Translational Medicine associated with Phosphoric diester hydrolases

0 Patents (Medical) associated with Phosphoric diester hydrolases

Literatures (Medical) associated with Phosphoric diester hydrolases

01 Sep 2010·New BiotechnologyQ2 · ENGINEERING & TECHNOLOGY

Effect of high hydrostatic pressure on the enzyme activities in Saccharomyces cerevisiae and Escherichia coli

Q2 · ENGINEERING & TECHNOLOGY

Article

Author: Hyun-Jung Chung ; Woo-Suk Bang

The purpose of this study was to evaluate the effect of high hydrostatic pressure (HHP) on the enzyme activities in Saccharomyces cerevisiae (ATCC 16664) and Escherichia coli (ATCC 11229). Enzyme activities before and after HHP treatment were determined using an APIZYME enzyme assay kit. Thirteen active enzymes were detected in S. cerevisiae and E. coli. Pressure treatment at 448 MPa for 30s at 23 degrees C resulted in different effects on enzymes in S. cerevisiae and E. coli. HHP completely inactivated lipase, cystine arylamidase, and chymotrypsin and moderately inactivated esterase, esterase lipase, leucine arylamidase, valine arylamidase and alpha-glucosidase in S. cerevisiae. In E. coli, esterase, esterase lipase, lipase, valine arylamidase, cystine arylamidase, trypsin, alpha-glucosidase, and beta-glucuronidase were completely inactivated and leucine arylamidase and beta-galactosidase retained partial activities. Phosphoric hydrolases were not inactivated in both microorganisms. The use of the enzyme assay kit provided rapid and useful information on the microorganisms' enzymes and their sensitivity to HHP treatment in a simple manner.

01 Aug 2002·Current Protocols in Toxicology

Assays for the Classification of Two Types of Esterases: Carboxylic Ester Hydrolases and Phosphoric Triester Hydrolases

Article

Author: Anspaugh, Douglas D. ; Roe, R. Michael

AbstractAssays for the Classification of Two Types of Esterases: Carboxylic Ester Hydrolase and Phosphoric Triester Hydrolase (Douglas D. Anspaugh and Michael Roe, North Carolina State University, Raleigh, North Carolina). This unit describes assays that quantitate two types of esterase the carboxylic ester hydrolases and the phosphoric triester hydrolases. Carboxylic ester hydrolases include the B‐esterases, which are inhibited by organophosphorus compounds. Among the phosphoric triester hydrolases is aryldialkylphosphatase, which has been called A‐esterase or paraoxonase due to its ability to oxidize paraoxon and other organophosphates. These assays are colorimetric and miniaturized for rapid simultaneous testing of multiple, small‐volume samples in a microtiter plate format. There is also a discussion of the history of esterase nomenclature and the reasons why this large group of enzymes is so difficult to classify.

01 Jan 2002·Diseases of Aquatic OrganismsQ3 · AGRICULTURAL & FORESTRY SCIENCE

Malabsorption syndrome observed in the common octopus Octopus vulgaris infected with Aggregata octopiana (Protista: Apicomplexa)

Q3 · AGRICULTURAL & FORESTRY SCIENCE

Article

Author: Pascual, S ; Gestal, C ; Páez de la Cadena, M

Octopus vulgaris infected with Aggregata octopiana were collected from an open-water culture system in the Ría of Aldán (NW Spain). Digestive tract infection values were determined with the use of a Neubauer chamber by counting the number of A. octopiana sporocysts. After determining enzyme activity values by the colorimetric Api-Zym system Biomerieux, one representative enzyme of glycosidases, peptid hydrolases and phosphoric hydrolases showing high activity was spectrophotometrically analysed. The enzymes were maltase and leucine-aminopeptidase (LAP) involved in the absorption process, and acid phosphatase, a lysosomic enzyme, respectively. Enzymatic activity of maltase and LAP decreased significantly, with increased sporocyst counts. However, acid phosphatase activity increased with severity of infection, indicating the presence of degradative enzymes from phagocytic cells in the infected area. A detrimental effect on gastrointestinal function may result from a decrease or malfunction of absorption enzymes. The results suggest a malabsorption syndrome resulting from parasitic infection.

Analysis

Perform a panoramic analysis of this field.

view full example data

Chat with Hiro

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, PatSnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

Phosphoric diester hydrolases

Basic Info

Related

Analysis