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Conclusion The recurrence rates of chronic rhinosinusitis (CRS) were higher in the aspirin nasal provocation test (ANPT)-positive group, regardless of the presence of nasal polyps. Thus, a careful endoscopic examination is required during follow-up in ANPT-positive patients with CRS. Objectives The aim of this study was to evaluate the clinical features and prognosis after surgical treatment in patients with CRS and aspirin hypersensitivity. Methods In a prospective study, 100 patients were analyzed with CRS who underwent endoscopic sinus surgery at the hospital from October 2012 to March 2013. This study measured changes in nasal volume and symptoms before and after the ANPT and examined patient's asthma history, allergy, Lund-Mackay score (LMS), total immunoglobulin E, percentage of peripheral eosinophils, and objectively measured relapse at 6 months. Results Patients wwith CRS and nasal polyps (CRSwNP) were more likely to have a positive ANPT test result compared to those without nasal polyps (CRSsNP) (21.4% vs 5.5%). The ANPT-positive group had a higher LMS and required more revision endoscopic sinus surgery than those in the ANPT-negative group. The results were that similar results were observed in CRSwNP and CRSsNP.

Chitosan has been investigated as a non‐viral vector because it has several advantages such as biocompatibility, biodegradability, and low toxicity. However, low specificity and low transfection efficiency of chitosan as a DNA carrier need to be overcome prior to clinical trial. In this review paper, chemical modification of chitosan was tried in order to enhance cell specificity and transfection efficiency. Also, chemical modification of chitosan was performed to increase stability of chitosan/DNA complexes.

Inulin fructotransferase (DFA III-producing) [EC 2.4.1.93] secreted from Bacillus sp. snu-7 was purified 60.3-fold with a yield of 11.6% from a culture supernatant by ammonium sulfate precipitation, preparative isoelectrofocusing, anion exchange chromatography and preparative polyacrylamide gel electrophoresis. The purified enzyme gave a single band on polyacrylamide gel electrophoresis. The molecular mass of the enzyme was estimated to be 62 kDa on SDS-polyacrylamide gel electrophoresis. The N-terminal amino acid sequence was found to be Ala-Asp-Gly-Gln-Asp-Gly-Ala-Pro-Leu-Asn-Gln-Val-Asn-Thr-Tyr-Asp. The optimal pH and temperature for the enzyme reaction were 6.0 and 40°C, respectively. The enzyme was stable with a pH range of 4.0 to 7.0 and at up to 60°C. As the production of di-D-fructose 1,2':2,3' dianhydride increased in the course of enzyme reaction, the Km of the purified enzyme was estimated to be 5.4 mM. One mM each of Cu(2+), Fe(2+) and Hg(2+) inhibited the enzyme activity strongly. Exhaustive enzymatic digestion of inulin produced 1-kestose, 1-nystose, and 1-F-fructofuranosylnystose as well as di-D-fructose 1,2':2,3' dianhydride.

The sequences of cDNA clones encoding the Bowman-Birk proteinase inhibitor (BBPI) and its isoinhibitors (D-II and C-II) have been identified. Nucleotide sequence homologies among these clones and between the two reactive domains in each clone were very high. These homologies suggest that the BBPI and its isoinhibitor genes may have evolved from a common ancestral inhibitor. Also, clone pB2 (D-II) had two identical reactive sites that inhibit trypsin only, and three repetitive regions that are about 81 bp and initiated with ATG. It was assumed from these results that isoinhibitor D-II was the most primordial type of these inhibitors.

A bestatin analogue, (2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-valine (AHPA-Val), from the culture filtrate of Streptomyces neyagawaensis SL-387 was obtained in a chemically defined medium containing DL-3-amino-3-phenylpropionic acid. AHPA-Val was 6 times (IC50 = 1.2 micrograms/ml) as strong as bestatin (IC50 = 7.0 micrograms/ml) against porcine kidney microsomal aminopeptidase N, and 4 times (5.6 micrograms/ml) as strong as bestatin (IC50 = 20.7 micrograms/ml) against aminopeptidase N of human metastatic fibrosarcoma HT1080. To the best of our knowledge, this is the first report on the microbial production of AHPA-Val.