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  • 1
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1193-1197 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Acuthrombin-B, a thrombin-like enzyme from Agkistrodon acutus venom, has been isolated and purified to homogeneity by ion-exchange chromatography on DEAE-Sepharose, gel filtration on Sephacryl S-100 and fast performance liquid chromatography on DEAE-8HR. The protease is an acid protein (pI 6.0) consisting of two non-identical polypeptide chains (14.4 and 16 kDa) and there is no disulfide bond between the subunits. Its molecular weight is 27 kDa as estimated by gel filtration on Sephacryl S-100. The protease has arginine-esterase activity and hydrolyzes synthetic substrates such as p-toluenesulfonyl arginine methyl ester and α-N-benzoyl-L-arginine amide ethyl ester, and shows clotting activity with human fibrinogen, rabbit citrated plasma and human citrated plasma in vitro. The specific activity with human fibrinogen was estimated to be 230 NIH units mg−1. The protease is considered as a serine-type protease and contains metal ion(s) to some extent, as indicated by the fact that its clotting and arginine-esterase activities could be completely inhibited by PMSF and partially inhibited by the chelating agent EDTA, while the thrombin inhibitor heparin had no effect on its clotting activity towards rabbit citrated plasma. Acuthrombin-B crystals with a resolution limit of 2.06 Å were obtained by conventional hanging-drop vapour diffusion. The crystals belong to space group P21 with unit-cell parameters a = 34.97, b = 53.58, c = 67.88 Å, β = 98.89° and contain one molecule per asymmetric unit.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Plant, cell & environment 7 (1984), S. 0 
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A generalized model of the higher plant body is proposed in order to assemble the discrete knowledge of the actions, and sites of biosynthesis, of phytohormones. In this model, we attempt to explain the differential sensitivities of different tissues. With this model most effects of plant hormones appear to be reasonable, and even expected. The model is based on a new anatomical and physiological classification of plant tissue. In higher plants the integration of an outer-inner polarity and an upper-lower polarity plays a major role in phytohormone behaviour.Plant tissues and organs which are derived from the cortex of paleophytes (the bud, the mesophyll of the leaf, the cortex of the stem, and the root cap) are classified as the outer pole of the plant. On the other hand, tissues and organs which are derived from the stele of paleophytes (the root, the stele of the shoot, and the vein of the leaf), are classified as the inner pole. It is suggested that tissue sensitivities to phytohormones are mainly determined by the outer-inner polarity. Phytohormones which are synthesized from one pole act on the other, whereas they exert either much less or no effect, or an inverse effect on their own pole. This is shown for both promoters and inhibitors of the phytohormones for both cortical and stelar vegetative tissues of plants.
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  • 3
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A three-phase partitioning method to separate indolyl-3-acetic acid (IAA) and abscisic acid (ABA) from a crude plant extract was developed and evaluated. The aqueous phase at pH 2.7 of a methanolic plant extract constituted the 1st phase, from which IAA and ABA were transferred via diethyl ether, the 2nd phase, to a 3rd phase consisting of an alkaline buffer, enclosed in a dialysis tube. Partitioning of the free forms of the two hormones among the three phases in one container were carried out simultaneously and efficiently. The method also proved to be satisfactory when used as a combined step for both extraction and partitioning, at which the plant homogenate in buffer at pH 2.7 constituted the 1st phase. The content of IAA and ABA in kernels of Zea mays and in hypocotyls of Beta vulgaris were tested with the new method. The method presented is reliable and time-saving, and the demand for chemicals is less than for most of the conventional procedures used.
    Type of Medium: Electronic Resource
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  • 4
    Publication Date: 1984-03-01
    Print ISSN: 0140-7791
    Electronic ISSN: 1365-3040
    Topics: Biology
    Published by Wiley
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  • 5
    Publication Date: 1999-06-01
    Description: Acuthrombin-B, a thrombin-like enzyme from Agkistrodon acutus venom, has been isolated and purified to homogeneity by ion-exchange chromatography on DEAE-Sepharose, gel filtration on Sephacryl S-100 and fast performance liquid chromatography on DEAE-8HR. The protease is an acid protein (pI 6.0) consisting of two non-identical polypeptide chains (14.4 and 16 kDa) and there is no disulfide bond between the subunits. Its molecular weight is 27 kDa as estimated by gel filtration on Sephacryl S-100. The protease has arginine-esterase activity and hydrolyzes synthetic substrates such as p-toluenesulfonyl arginine methyl ester and α-N-benzoyl-L-arginine amide ethyl ester, and shows clotting activity with human fibrinogen, rabbit citrated plasma and human citrated plasma in vitro. The specific activity with human fibrinogen was estimated to be 230 NIH units mg−1. The protease is considered as a serine-type protease and contains metal ion(s) to some extent, as indicated by the fact that its clotting and arginine-esterase activities could be completely inhibited by PMSF and partially inhibited by the chelating agent EDTA, while the thrombin inhibitor heparin had no effect on its clotting activity towards rabbit citrated plasma. Acuthrombin-B crystals with a resolution limit of 2.06 Å were obtained by conventional hanging-drop vapour diffusion. The crystals belong to space group P21 with unit-cell parameters a = 34.97, b = 53.58, c = 67.88 Å, β = 98.89° and contain one molecule per asymmetric unit.
    Print ISSN: 0907-4449
    Electronic ISSN: 1399-0047
    Topics: Chemistry and Pharmacology , Geosciences , Physics
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