A new species of Goniothalamus (Annonaceae) from New Caledonia, representing a significant range extension for the genus

A previously unknown Annonaceae species from the South Pacific island of New Caledonia is described as Goniothalamus dumontetii . This is the first Goniothalamus species reported from the island, and the easternmost record for the genus. It is easily distinguished from its congeners by the shape of the monocarp (flattened elongate with lateral triangular projections), which reflects the shape of the seeds (flattened rhombohedral). The conservation status of the species is evaluated as endangered (EN) using World Conservation Union (IUCN) red list categories, as it is known from only one relatively small population. The interpretation of geological and molecular data suggests that Goniothalamus dispersed to New Caledonia relatively recently, and does not represent a relict of the break-up of Gondwana.  © 2007 The Linnean Society of London, Botanical Journal of the Linnean Society , 2007, 155 , 497–503.     

Physicochemical properties of proteins from wheat grown under high-contrast climatic conditions

Studies using electrophoresis, gel chromatography, viscometry, and calorimetry revealed an interrelation of several physicochemical properties of proteins of soft wheat grown under conditions of cool and wet weather with rheological characteristics of gluten and dough and bread quality. The ratio of gliadin and albumin-globulin polypeptides in flour with short-tearing gluten was much lower compared to that in flour with normal gluten. Proteins from flour with short-tearing gluten, including the water-soluble and salt-soluble fraction, had a loose spatial structure. Gluten fractions of this gluten (gliadin and glutenin) were characterized by a more compact and elongated structure compared to normal gluten. As distinct from normal gluten, the conformation of protein particles in short-tearing gluten depended little on hydrophobic interactions. The results suggest that the main components of grain determine the rheological properties of short-tearing gluten.     

一种钒配合物LMC 抑制DNA 拓扑异构酶?的抗肿瘤作用

目的：探讨钒配合物LMc对拓扑异构酶Ⅰ、Ⅱ（Topo-Ⅰ、Topo-Ⅱ）的影响及其抗肿瘤活性。方法：采用DNA松弛实验观察LMC对Topo-Ⅰ、活性的影响并探讨其相关分子作用机制;采用MTT法、流式细胞术在细胞水平观察了IMC的抗肿瘤作用。结果：LMC可明显抑制Topo-Ⅰ活性,对Topo-Ⅱ无明显抑制作用,对多种肿瘤细胞株A549、Hela、BEL-7402具有明显抑制生长的作用,且可将细胞阻断在G2／M期,而对正常细胞株L-02生长无明显影响。结论：钒配合物LMC具有抑制Topo-Ⅰ活性而发挥抗肿瘤的作用。     

Interactions of neural glycosaminoglycans and proteoglycans with protein ligands: assessment of selectivity, heterogeneity and the participation of core proteins in binding

The method of affinity coelectrophoresis was used to study the binding of nine representative glycosaminoglycan (GAG)-binding proteins, all thought to play roles in nervous system development, to GAGs and proteoglycans isolated from developing rat brain. Binding to heparin and non-neural heparan and chondroitin sulfates was also measured. All nine proteins-laminin-1, fibronectin, thrombospondin-1, NCAM, L1, protease nexin-1, urokinase plasminogen activator, thrombin, and fibroblast growth factor-2-bound brain heparan sulfate less strongly than heparin, but the degree of difference in affinity varied considerably. Protease nexin-1 bound brain heparan sulfate only 1.8- fold less tightly than heparin (Kdvalues of 35 vs. 20 nM, respectively), whereas NCAM and L1 bound heparin well (Kd approximately 140 nM) but failed to bind detectably to brain heparan sulfate (Kd>3 microM). Four proteins bound brain chondroitin sulfate, with affinities equal to or a few fold stronger than the same proteins displayed toward cartilage chondroitin sulfate. Overall, the highest affinities were observed with intact heparan sulfate proteoglycans: laminin-1's affinities for the proteoglycans cerebroglycan (glypican-2), glypican-1 and syndecan-3 were 300- to 1800-fold stronger than its affinity for brain heparan sulfate. In contrast, the affinities of fibroblast growth factor-2 for cerebroglycan and for brain heparan sulfate were similar. Interestingly, partial proteolysis of cerebroglycan resulted in a >400- fold loss of laminin affinity. These data support the views that (1) GAG-binding proteins can be differentially sensitive to variations in GAG structure, and (2) core proteins can have dramatic, ligand-specific influences on protein-proteoglycan interactions.      

The concentration of antibodies to several exoenzymes of beta-hemolytic streptococci in commercial preparations of gamma globulin]

For the purpose of possible use of commercial preparations of homologous gamma-globulin in the outbreaks of streptococcus affections the authors studied the content of antibodies to some streptococcus antigens, namely to O-streptolysin, streptohyaluronidase and streptokinase. High antibody titres to streptokinase were observed in 62.7, to O-streptolysin--in 35.2 and to streptohyaluronidase--in 15.4% of the batches under study. The greatest amount of antibodies to all the antigens under study was revealed in gamma-globulin prepared from the blood sera collected during the automno-winter period of the year.     

Regulation of purified NAD-isocitrate dehydrogenase from the pig heart by calcium ions and cAMP-dependent protein kinase

Different cAMP-dependent protein kinases do not phosphorylate homogeneous NAD-isocitrate dehydrogenase (ICDH) and do not change its activity. Ca2+ (3 X 10(-7) = 10(-3) M) activates the enzyme throughout the process of purification including homogeneous enzyme by decreasing the KM for isocitrate. The calmodulin inhibitor trifluoperazine does not change ICDH activation.