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Ja Young Moon

Publications and source records attributed to Ja Young Moon.

2 recordsLinked to original sources

Botulinum toxin type A for poststroke cricopharyngeal muscle dysfunction.

OBJECTIVE: To evaluate the therapeutic effectiveness of botulinum toxin type A (BTX-A) in poststroke patients with cricopharyngeal muscle dysfunction. DESIGN: Before-after trial. SETTING: University hospital. PARTICIPANTS: Eight poststroke patients. INTERVENTION: BTX-A injection into the cricopharyngeal muscle under endoscope guidance for poststroke cricopharyngeal muscle dysfunction. MAIN OUTCOME MEASURES: Clinical symptom score, disability rating scale for swallowing impairment, videofluoroscopic swallowing study, and upper esophageal sphincter (UES) manometry. RESULTS: Clinical symptom score, disability rating scale for swallowing impairment, residue in piriform sinus, and UES pressure were all significantly improved at 2 weeks after BTX-A injection compared with evaluations before injection (P<.05). The effects on the clinical symptom score and disability rating scale for swallowing impairment continued to be significantly improved to 12 weeks after injection (P<.05). However, the residue in piriform sinus and the UES pressure at 12 weeks postinjection were reduced compared with before-injection evaluations; these results were not significant. The pharyngeal transit time was not changed after injection. There were no side effects observed in the patients studied. CONCLUSIONS: The results of the present study suggest that BTX-A injection may be an effective and safe treatment in patients with poststroke cricopharyngeal muscle dysfunction.

Aged↗

Purification and characterization of ascorbic acid 2-kinase from Flavobacterium devorans ATCC 10829.

Maximum activity for phosphorylating C(2)-OH of the ascorbic acid was observed at the time of 16 h incubation from the culture of Flavobacterium devorans ATCC 10829. The enzyme was purified 1.178-fold, via ammonium sulfate fractionation, Fast Q anion exchange, and phenyl agarose chromatography. Gel chromatography and SDS-polyacrylamide electrophoresis experiments showed that the enzyme is a tetramer with subunit MW of 29 kDa. Among available second substrates, pyrophosphate showed the highest activity. Optimum temperature and pH were 45 degrees C and 5.5, respectively. The enzyme was chemically modified only by diethylpyrocarbonate and 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC), indicating that histidine and carboxylate are in the active site. pH studies showed that two histidines are involved in the binding of the substrates and a carboxylate in catalysis. Therefore, the chemical mechanism of the enzyme is likely that two histidines bind to pyrophosphate and carboxylate, respectively, and a carboxylate acts as a general base.

Ascorbic Acid↗