Matrix metalloproteinase–inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors

We structurally characterized the adducts of the catalytic domain of matrix metalloproteinase-3 (MMP3) with three different nonpeptidic inhibitors by solving the solution structure of one adduct [MMP3–N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid] and then by calculating structural models of the other two adducts using a reduced set of experimental NMR data, following a recently proposed procedure (Bertini et al. in J. Med. Chem. 48:7544–7559, 2005). The inhibitors were selected with the criteria of maintaining in all of them the same zinc-coordinating moiety and of selectively changing the substituents and/or the functional groups. The backbone dynamics on various time scales have been characterized as well. The comparison among these structures and with others previously reported allowed us to elucidate fine details of inhibitor–receptor interactions and to develop some criteria, which could guide in optimizing the design of selective inhibitors. Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users.     

Immunochemical and immunohistochemical detection of S-100-like immunoreactivity in spinach tissues.

S-100 proteins represent a group of closely related acidic, calcium binding proteins originally isolated from the mammalian nervous system and later detected in non-neural cell types and in a wide variety of vertebrate and invertebrate species. The present study used immunochemical and immunohistochemical methods to extend the investigation of S-100 during phylogenesis to plant tissues. The presence of S-100-like immunoreactive material was detected in extracts of spinach (Spinacia oleracea L.) terminal buds and young leaves by the ELISA method and by Western blotting using different anti-S-100 rabbit antisera. Using the PAP method, serial sections of young spinach leaves treated with the same antisera exhibited an immunoreaction product that was confined to the cytoplasm and nucleus (but absent from the vacuoles) in meristematic, epidermal, and parenchymal cells. The present data enlarge the field of investigation of S-100 proteins in the search of the function(s) of S-100 in biological organisms.     

H NOE studies of oxidized high potential iron sulfur protein II from Ectothiorhodospira halophila

The ¹H NMR spectra of oxidized HiPIP II from Ectothiorhodospira halophila have been recorded at 600 MHz. Nuclear Overhauser effect measurements have allowed the assignment of the cysteine β-CH₂ resonances. Four β-CH₂ signals are downfield shifted and four upfield shifted. Through a theoretical model and on the ground of Mössbauer data on analogous systems we propose that the upfield signals are those of the cysteines bound to the iron(III) ions and those downfield of the cysteines bound to the mixed valence pair Fe(III)-Fe(II).     

Induction of indoleamine dioxygenase by interferon in mice: a study with different recombinant interferons and various cytokines

Since it is important the availability of a specific marker for interferon induction in vivo, we investigated the effect of different recombinant interferons and various cytokines on indoleamine 2,3-dioxygenase activity. Although with different magnitude, recombinant interferon-alpha A/D (Bgl II) hybrid, interferon-gamma and tumor necrosis factor, all increase the activity of this enzyme, whereas interleukin-1, recombinant interferon-alpha A and interferon-alpha D do not induce this activity in mice lung tissue. Dexamethasone is able to inhibit indoleamine 2,3-dioxygenase induction by lipopolysaccharide or by interferon-alpha A/D but it fails to prevent the induction by interferon-gamma.     

Quantitative estimation of gibberellic acid by paper chromatography

Метод для количественного определения от gibberellic кислоты в процессе брожения средства массовой информации, с использованием бумаги по убыванию хроматографии в butylacetate воды описана. Образца корректируется, чтобы рН 2.5-3.0, добыто с н-бутанола, и 0,05 мл. органического слоя пятнами на Хроматографический бумагу. После equilibration от Атмосфера в банке, chromatogram Разработана в butylacetate насыщенных с водой, за 7 часов, и растворитель разрешено покинуть капельного нижней части листа. Обнаружение осуществляется путем опрыскивания с 3% раствор серной кислоты в метаноле и после сушки бумаги, пятна с синий u.v. флуоресценции наблюдается. Определенный артикль площадь пятна оценивается с помощью калибровочной кривой, заговор с ценностей, стандартов, соответствующих 20, 60 и 120 μ g. gibberellic кислоты. Погрешность оценки составляет ± 10-15% когда оценки выполняются тщательно. Низкий предел чувствительности 5 μg.