67336-99-6 Usage
Uses
Used in Research and Clinical Applications:
Z-GLY-PRO-BETANA is used as a substrate in enzymatic studies and experiments for its ability to mimic natural peptides and facilitate the investigation of enzymatic activities and mechanisms.
Used in Pharmaceutical Development:
Z-GLY-PRO-BETANA is utilized as a lead compound in the development of new pharmaceuticals due to its potential therapeutic properties, including anti-inflammatory and antioxidant effects, which are beneficial in the treatment of various diseases and conditions.
Used in Disease and Condition Studies:
Z-GLY-PRO-BETANA is employed as a research tool to study the pathophysiology of different diseases and conditions, given its potential therapeutic effects and its ability to interact with biological systems.
Used in Drug Delivery Systems:
In the pharmaceutical industry, Z-GLY-PRO-BETANA may be used as a component in drug delivery systems to improve the bioavailability and efficacy of therapeutic agents, leveraging its properties to enhance drug targeting and reduce side effects.
Used in Cosmetics and Personal Care:
Given its potential anti-inflammatory and antioxidant properties, Z-GLY-PRO-BETANA could be incorporated into cosmetics and personal care products to provide skin health benefits and protect against environmental stressors.
Used in Nutritional Supplements:
Z-GLY-PRO-BETANA may be used as an ingredient in nutritional supplements to support general health and well-being, capitalizing on its potential health-promoting effects.
Check Digit Verification of cas no
The CAS Registry Mumber 67336-99-6 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 6,7,3,3 and 6 respectively; the second part has 2 digits, 9 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 67336-99:
(7*6)+(6*7)+(5*3)+(4*3)+(3*6)+(2*9)+(1*9)=156
156 % 10 = 6
So 67336-99-6 is a valid CAS Registry Number.
67336-99-6Relevant academic research and scientific papers
POST-PROLINE ENDOPEPTIDASE. PARTIAL PURIFICATION AND CHARACTERIZATION OF THE ENZYME FROM PIG KIDNEYS
Hauzer, Karel,Servitova, Linda,Barth, Tomislav,Jost, Karel
, p. 1139 - 1148 (2007/10/02)
Post-proline endopeptidase was isolated from pig kidneys and partially purified.The procedure consisted of fractionation with ammonium sulphate, ion exchange chromatography on DEAE-Sephadex A-50, gel filtration on Sephadex G-200 and rechromatography on DEAE-Sephadex A-50.The preparation had 55 times higher specific activity than the crude extract and did not contain any contaminating enzymic activities.The enzyme cleaved a number of proline-containing peptides and was strictly specific in catalyzing the hydrolysis of the peptide bond on the carboxyl side of the proline residue.The optimum pH for the hydrolysis of the synthetic peptides benzyloxycarbonylglycyl-prolyl-leucyl-glycinamide and benzyloxycarbonyl-glycyl-proline β-naphthylamide was 7.8-8.0 and, in the case of benzyloxycarbonylglycyl-proline p-nitroanilide, 7.2 to 7.5.For the hydrolysis of the tetrapeptide benzyloxycarbonylglycyl-prolyl-leucyl-glycinamide, the Km value of 75 μmol l-1 was obtained.
