(S)-(-)-PROPRANOLOLHYDROCHLORIDE

[ Density]:
1.475 g/cm3

[ Boiling Point ]:
319.2ºC at 760 mmHg

[ Melting Point ]:
290ºC (dec.)(lit.)

[ Molecular Formula ]:
C₂H₈NO₃P

[ Molecular Weight ]:
125.06400

[ Flash Point ]:
146.9ºC

[ Exact Mass ]:
125.02400

[ PSA ]:
93.36000

[ LogP ]:
0.16910

[ Index of Refraction ]:
1.495

Click to get detail MSDS

[ Symbol ]:

GHS07

[ Signal Word ]:
Warning

[ Hazard Statements ]:
H315-H319-H335

[ Precautionary Statements ]:
P261-P305 + P351 + P338

[ Personal Protective Equipment ]:
dust mask type N95 (US);Eyeshields;Gloves

[ Hazard Codes ]:
Xi: Irritant;

[ Risk Phrases ]:
R36/37/38

[ Safety Phrases ]:
26-37/39

[ RIDADR ]:
NONH for all modes of transport

[ HS Code ]:
2931900090

Click to get detail synthetic route

Precursor

DownStream

[ HS Code ]: 2931900090

[ Summary ]:
2931900090. other organo-inorganic compounds. VAT:17.0%. Tax rebate rate:13.0%. Supervision conditions:AB(certificate of inspection for goods inward,certificate of inspection for goods outward). MFN tariff:6.5%. General tariff:30.0%

Synthesis and structure-activity relationships of antibacterial phosphonopeptides incorporating (1-aminoethyl)phosphonic acid and (aminomethyl)phosphonic acid.

J. Med. Chem. 29 , 29, (1986)

Phosphonodipeptides and phosphonooligopeptides based on L- and D-(1-aminoethyl)phosphonic acids L-Ala(P) and D-Ala(P) and (aminomethyl)phosphonic acid Gly(P) at the acid terminus have been synthesized...

Slow-binding and competitive inhibition of 8-amino-7-oxopelargonate synthase, a pyridoxal-5'-phosphate-dependent enzyme involved in biotin biosynthesis, by substrate and intermediate analogs. Kinetic and binding studies.

Eur. J. Biochem. 259(1-2) , 63-70, (1999)

8-Amino-7-oxopelargonate synthase catalyzes the first committed step of biotin biosynthesis in micro-organisms and plants. Because inhibitors of this pathway might lead to antibacterials or herbicides...

[Kinetic characteristics and enantioselective action of penicillinase in the hydrolysis reaction of N-phenylacetyl derivatives of 1-aminoethylphosphonic acid and its esters].

Biokhimiia 55(6) , 1124-31, (1990)

Penicillin acylase from E. coli (EC 3.5.1.11) was found to hydrolyze N-phenylacetylated 1-aminoethylphosphonic acid and its esters. The enzyme preferentially converts the R-form of the substrates: the...

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