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We describe the synthesis and photophysical properties of 11 substituted 5-(benzothiazol-2-yl)-2Ј-deoxyuridine derivatives and oligodeoxyribonucleotides (ODNs) containing 5-(5,6-dimethoxybenzothiazol-2-yl)-2Ј-deoxyuridine (d

Chemoselectivity in DNA: The thymidine lesion 5‐formyl‐2′‐deoxyuridine (1) induces the mutation of DNA. Its derivatization with the specific fluorogenic reagent 2‐amino‐4,5‐dimethoxythiophenol (2) gives 3, which shows strong fluorescence. This fast method for the detection of 1 requires no enzymatic digestion, HPLC separation, or MS analysis. ROS=reactive oxygen species.

High prolyl endopeptidase (post-proline cleaving enzyme) [EC 3.4.21.26] activity was detected in fruit bodies of shakashimeji (Lyophyllum cinerascens), tsukuritake (mushroom: Agaricus bisporus), hirohachichitake (Lactarius hygrophoroides), and yaburebenitake (Russula lepida) which belong to the genus Basidiomycetes. Cell-free extract of shakashimeji showed high activities of proline iminopeptidase and arylamidase as well as prolyl endopeptidase. The prolyl endopeptidase was purified from the extract of shakashimeji by sequential chromatographies on DEAE-Toyopearl, DEAE-Sephadex and hydroxyapatite, and high-performance liquid chromatography with a DEAE-5PW column. The purified enzyme was homogeneous as judged by disc gel electrophoresis. The enzyme was most active at pH 6.8 as checked with Z-Gly-Pro-beta-naphthylamide as a substrate and was stable in the range of pH 5.8-7.4. The isoelectric point of the enzyme was 5.2 and the molecular weight was estimated to be 76,000 by gel filtration on Sephadex G-150 and by sodium dodecyl sulfate (SDS) gel electrophoresis, suggesting that the enzyme was a monomer. The enzyme was completely inhibited by diisopropyl fluorophosphate (DFP), Z-Gly-Pro-CH2Cl, and Z-Pro-prolinal, while it was not inhibited by p-chloromercuribenzoate (PCMB), phenylmethylsulfonyl fluoride (PMSF), or metal chelators. It was estimated that at least five subsites were concerned with the enzyme-substrate binding. Among them, the S1, S2, and S1' sites showed high stereospecificity, as in mammalian, microbial, and plant enzymes. The enzyme hydrolyzed TRH at the carboxyl side of the proline residue. The mushroom enzyme, that was sensitive to DFP, Z-Pro-prolinal, and Z-Gly-Pro-CH2Cl, but not to PCMB, were quite similar in characteristics to the Flavobacterium enzyme.(ABSTRACT TRUNCATED AT 250 WORDS)

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Plasma levels of az-plasmin inhibitor (a2PI) and a,-plasmin inhibitor-plasmin complex (a2PlPC) were measured by sandwich enzyme-linked immunosorbent assay, using a recently developed monoclonal anti-a2PI antibody, in patients with collagen diseases. Twenty patients had systemic lupus erythematosus (SLE), 4 of whom also had vasculitis, 11 patients had rheumatoid arthritis (RA), 4 of whom also had vasculitis, and 5 patients had other types of vasculitis. There was no significant difference in azPl levels between the 3 patient groups and the control groups. However, plasma levels of a,PIPC in all 3 patient groups were significantly higher than those in the control group. Moreover, plasma concentrations of a2PIPC in SLE patients with vasculitis were statistically significantly higher than those in SLE patients without vasculitis. These concentrations were also higher in RA patients with vasculitis than in RA patients without vasculitis, although the difference was not statistically significant. Our findings indicate that measurement of plasma %PIPC levels is useful for detecting and evaluating the severity and activity of vasculitis in patients with collagen diseases.

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