18684-24-7

Basic information

• Product Name: H-PRO-HYP-OH
• Synonyms: PRO-HYDROXY-PRO;H-PRO-HYP-OH;L-PRO-HYPRO-PRO;(2S,4R)-4-hydroxy-1-[(2S)-pyrrolidine-2-carbonyl]pyrrolidine-2-carboxylic acid;Prolylhydroxyproline;(2S,4R)-4-hydroxy-1-((S)-pyrrolidine-2-carbonyl)pyrrolidine-2-carboxylic acid;Dipeptide-6;4-Hydroxy-1-L-prolyl-L-proline
• CAS NO: 18684-24-7
• Molecular Formula: C10H16N2O4
• Molecular Weight: 228.25
• EINECS: 242-609-6
• Mol File: 18684-24-7.mol

Chemical Properties

• Boiling Point: 513.456 °C at 760 mmHg
• Flash Point: 264.329 °C
• Appearance: /
• Density: 1.417 g/cm³
• Refractive Index: 1.586
• Storage Temp.: -15°C
• CAS DataBase Reference: H-PRO-HYP-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-PRO-HYP-OH(18684-24-7)
• EPA Substance Registry System: H-PRO-HYP-OH(18684-24-7)

Safety Data

• Hazardous Substances Data: 18684-24-7(Hazardous Substances Data)

Usage

Chemical Properties

White powder

InChI:InChI=1/C10H16N2O4/c13-6-4-8(10(15)16)12(5-6)9(14)7-2-1-3-11-7/h6-8,11,13H,1-5H2,(H,15,16)/t6?,7-,8?/m0/s1

Upstream product

• 55878-58-5 Cbz-Pro-Hyp-OH 
• 2239-67-0 Gly-Pro-Hyp 

Relevant articles and documents

Collagen peptide, dipeptide and malady inhibitor

A problem that the present invention is to solve is to provide: a main body of a peptide molecule which is effective for inhibition of various maladies such as osteoporosis, osteoarthritis and pressure ulcer, particularly, a dipeptide which is easy to absorb into a body in an intestine; a collagen peptide which comprises the dipeptide as an essential dipeptide; and a malady inhibitor which comprises the dipeptide as an essential effective component. As a means of solving such a problem, a collagen peptide according to the present invention is characterized by comprising a dipeptide having a structure of Hyp-Gly as an essential dipeptide. A dipeptide according to the present invention is characterized by having a structure of Hyp-Gly. A malady inhibitor according to the present invention is characterized by comprising a dipeptide having a structure of Hyp-Gly as an essential effective component.

Inhibition and metal ion activation of pig kidney aminopeptidase P. Dependence on nature of substrate

Pig kidney aminopeptidase P (AP-P; EC 3.4.11.9) has been purified to homogeneity after its solubilisation from brush border membranes by phosphatidylinositol-specific phospholipase C. The effects of various activators and inhibitors of AP-P activity have been examined with a number of different substrates for the enzyme. The hydrolysis of bradykinin and ArgProPro is inhibited at Mn2+ concentrations above 10-5 M, whereas the hydrolysis of other substrates (GlyProHyp, β-casomorphin, substance P) is substantially activated, with 4-10 mM Mn2+ being optimal. The thiol reagent, p-chloromercuriphenylsulphonic acid, inhibits the hydrolysis of GlyProHyp but markedly activates the hydrolysis of bradykinin. A number of inhibitors of angiotensin converting enzyme (ACE; EC 3.4.15.1), previously reported to inhibit the hydrolysis of GlyProHyp, have no effect on the hydrolysis of bradykinin except in the presence of Mn2+. Differences were also observed in the degree of inhibition of GlyProHyp and bradykinin hydrolysis by EDTA and their reactivation by divalent cations. The hydrolysis of GlyProHyp follows Michaelis-Menten kinetics with a K(m) value of 2.7 mM. Bradykinin inhibits GlyProHyp hydrolysis with an I50 of 1.4 μM. The hydrolysis of bradykinin by AP-P reveals anomalous nonlinear kinetics indicative of negative cooperativity or the presence of more than one active site for this substrate. These results indicate that substrates for AP-P can be divided into 2 groups based on their responses to inhibitors and cation activators.