PubMed Health⌕ Search

PubMed · 11576763

UV absorption method should not be applied for determining amoxycillin in acidic dissolution test medium.

Abstract

In order to clarify the suitability of assay method, the stability of amoxycillin (AMX) in the acidic solution at pH 1.2 was determined by two different methods, ultraviolet absorption (UV) and HPLC methods. The determination was simultaneously performed for the same sample solutions. The data from HPLC method indicated that AMX degraded and the concentration of AMX in the acidic solution was decreased. The apparent first-order rate constant (k(obs)) for the degradation was 9.83x10(-2) h(-1), and the half-life was calculated to be 7.04 h. On the other hand, the data obtained from UV method apparently represented that the concentration of AMX increased with time-course. This phenomena was brought about by the increase of UV absorption at 272 nm, which accompanied with the degradation of AMX. These results clearly indicate that UV method can not be used for determining the samples accompanying the degradation of AMX. In general, the dissolution test (drug release test) has been used for the evaluation of a sustained-release dosage form of AMX. It is impossible to avoid the degradation of AMX in the test under acidic conditions. The results indicated that the UV method should not be used for the determination of AMX in the test.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

T Tokumura, Y Machida. 2001-10-09. UV absorption method should not be applied for determining amoxycillin in acidic dissolution test medium.. https://doi.org/10.1016/s0378-5173(01)00837-7

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies.

Exposure of antibodies to low pH is often unavoidable for purification and viral clearance. The conformation and stability of two humanized monoclonal antibodies (hIgG4-A and -B) directed against different antigens and a mouse monoclonal antibody (mIgG1) in 0.1M citrate at acidic pH were studied using circular dichroism (CD), differential scanning calorimetry (DSC), and sedimentation velocity. Near- and far-UV CD spectra showed that exposure of these antibodies to pH 2.7-3.9 induced only limited conformational changes, although the changes were greater at the lower pH. However, the acid conformation is far from unfolded or so-called molten globule structure. Incubation of hIgG4-A at pH 2.7 and 3.5 at 4 degrees C over the course of 24 h caused little change in the near-UV CD spectra, indicating that the acid conformation is stable. Sedimentation velocity showed that the hIgG4-A is largely monomeric at pH 2.7 and 3.5 as well as at pH 6.0. No time-dependent changes in sedimentation profile occurred upon incubation at these low pHs, consistent with the conformational stability observed by CD. The sedimentation coefficient of the monomer at pH 2.7 or 3.5 again suggested that no gross conformational changes occur at these pHs. DSC analysis of the antibodies showed thermal unfolding at pH 2.7-3.9 as well as at pH 6.0, but with decreased melting temperatures at the lower pH. These results are consistent with the view that the antibodies undergo limited conformational change, and that incubation at 4 degrees C at low pH results in no time-dependent conformational changes. Titration of hIgG4-A from pH 3.5 to 6.0 resulted in recovery of native monomeric proteins whose CD and DSC profiles resembled those of the original sample. However, titration from pH 2.7 resulted in lower recovery of monomeric antibody, indicating that the greater conformational changes observed at this pH cannot be fully reversed to the native structure by a simple pH titration.

Acids↗

NAADP induces pH changes in the lumen of acidic Ca2+ stores.

NAADP (nicotinic acid-adenine dinucleotide phosphate)-induced Ca2+ release has been proposed to occur selectively from acidic stores in several cell types, including sea urchin eggs. Using fluorescence measurements, we have investigated whether NAADP-induced Ca2+ release alters the pH(L) (luminal pH) within these acidic stores in egg homogenates and observed their prompt, concentration-dependent alkalinization by NAADP (but not beta-NAD+ or NADP). Like Ca2+ release, the pH(L) change was desensitized by low concentrations of NAADP suggesting it was secondary to NAADP receptor activation. Moreover, this was a direct effect of NAADP upon the acidic stores and not secondary to increases in cytosolic Ca2+ as it was not mimicked by IP3 (inositol 1,4,5-trisphosphate), cADPR (cyclic adenine diphosphoribose), ionomycin, thapsigargin or by direct addition of Ca2+, and was not blocked by EGTA. The results of the present study further support acidic stores as targets for NAADP and for the first time reveal an adjunct role for NAADP in regulating the pH(L) of intracellular organelles.

Acids↗

Acid-promoted cyclization reactions of tetrahydroindolinones. Model studies for possible application in a synthesis of selaginoidine.

The synthesis of various substituted bicyclic lactams by an acid-induced Pictet-Spengler reaction of tetrahydroindolinones bearing tethered heteroaromatic rings is presented. The outcome of the cyclization depends on the position of the furan tether, tether length, nature of the tethered heteroaromatic ring, and the substituent group present on the 5-position of the tethered heteroaryl group. A one-pot procedure was developed to efficiently prepare tetrahydroindolinones containing tethered furan rings. In a typical example, the reaction of furanyl azide 26 with n-Bu3P delivered iminophosphorane 27, which was allowed to react with a 1-alkyl-(2-oxocyclohexyl)acetic acid to provide the desired furanyl-substituted tetrahydroindolinone system 29. Treatment of 29 with trifluoroacetic acid afforded the tetracyclic lactam skeleton 30 found in the alkaloid (+/-)-selaginoidine.

Acids↗