23315-18-6 Usage
Description
SulbactaM M-1, also known as 3-Sulfino-D-valine, is a compound that acts as an effective scavenger of hypochlorous acid (HOCl). It is recognized for its therapeutic effects, which are believed to be due to its ability to protect tissues against the reactive HOCl released by activated granulocytes at inflammation sites.
Uses
Used in Pharmaceutical Industry:
SulbactaM M-1 is used as an active pharmaceutical ingredient for its therapeutic effects in protecting tissues against reactive HOCl during inflammation. Its role as a scavenger of HOCl contributes to its potential use in treating conditions associated with inflammation and oxidative stress.
Used in Antioxidant Applications:
SulbactaM M-1 is used as an antioxidant agent for its ability to neutralize harmful reactive oxygen species, such as HOCl, which can cause cellular damage and contribute to various diseases. Its antioxidant properties make it a valuable compound in the development of therapeutic strategies to combat oxidative stress-related conditions.
Used in Inflammation Management:
SulbactaM M-1 is used as an anti-inflammatory agent due to its protective effects against the reactive HOCl released by activated granulocytes at inflammation sites. This property makes it a potential candidate for the development of treatments targeting inflammation-related disorders and conditions.
Check Digit Verification of cas no
The CAS Registry Mumber 23315-18-6 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,3,3,1 and 5 respectively; the second part has 2 digits, 1 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 23315-18:
(7*2)+(6*3)+(5*3)+(4*1)+(3*5)+(2*1)+(1*8)=76
76 % 10 = 6
So 23315-18-6 is a valid CAS Registry Number.
23315-18-6Relevant articles and documents
Steady-state substrate specificity and O2-coupling efficiency of mouse cysteine dioxygenase
Li, Wei,Pierce, Brad S.
, p. 49 - 56 (2015/02/19)
Cysteine dioxygenase (CDO) is a non-heme mononuclear iron enzyme that catalyzes the oxygen-dependent oxidation of l-cysteine (Cys) to produce l-cysteine sulfinic acid (CSA). Sequence alignment of mammalian CDO with recently discovered thiol dioxygenase enzymes suggests that the mononuclear iron site within all enzymes in this class share a common 3-His first coordination sphere. This implies a similar mechanistic paradigm among thiol dioxygenase enzymes. Although steady-state studies were first reported for mammalian CDO over 45 years ago, detailed analysis of the specificity for alternative thiol-bearing substrates and their oxidative coupling efficiencies have not been reported for this enzyme. Assuming a similar mechanistic theme among this class of enzymes, characterization of the CDO substrate specificity may provide valuable insight into substrate-active site intermolecular during thiol oxidation. In this work, the substrate-specificity for wild-type Mus musculus CDO was investigated using NMR spectroscopy and LC-MS for a variety of thiol-bearing substrates. Tandem mass spectrometry was used to confirm dioxygenase activity for each non-native substrate investigated. Steady-state Michaelis-Menten parameters for sulfinic acid product formation and O2-consumption were compared to establish the coupling efficiency for each reaction. In light of these results, the minimal substrate requirements for CDO catalysis and O2-activation are discussed.
