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  • 11
    Electronic Resource
    Electronic Resource
    Prevention of symptomatic vasospasm by topically applied Nimodipine (1982)
    Springer
    Acta neurochirurgica 63 (1982), S. 297-302 
    Details
    ISSN: 0942-0940
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A 2.4×10−5M solution of the Calcium-antagonist Nimodipine was administered to the exposed cerebral vessels in 17 patients intraoperatively clipping of a ruptured aneurysm. The interval between subarachnoid haemorrhage and operation was 48 to 72 hours. The CT investigation had revealed blood accumulation in the basal cisterns in all cases. Vasodilatation was observed in all instances; the percentage being greater in small vessels as compared to large vessels. Postoperatively, a neurological deficit combined with angiographically verified vasospasm occurred in two patients, but was reversible in both. Fifteen patients remained free from symptomatic vasospasm and were discharged without neurological deficit. In 13 of these patients and 3 additional cases, a plastic cannula was placed intraoperatively so that postoperative topical administration of Nimodipine was possible. Postoperative control-angiograms after a mean interval of 7 days from SAH did not show severe spasm in any of the patients; localised moderate asymptomatic spasm was found in 8 cases and was reserved in 5. Moderate postoperative symptomatic spasm was observed in 2 patients, treated and reversed in one patient. In 5 of 7 cases without evidence of spasm in the angiogram postoperative topical administration of Nimodipine caused vasodilatation. It is concluded, that topical intracisternal administration of Nimodipine reverses intraoperative vascular spasm and decreases the probability of postoperative symptomatic vasospasm after early surgery.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01728885
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  • 12
    Electronic Resource
    Electronic Resource
    Patterns of vegetative growth and reproduction in relation to branch orders: the plant as a spatially structured population (2000)
    Springer
    Trees 14 (2000), S. 329-333 
    Details
    ISSN: 0931-1890
    Keywords: Key words Vegetative growth ; Reproduction ; Spatially structured population ; Hierarchical allocation ; Opportunity cost
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract  The patterns of vegetative growth and reproduction in relation to orders of terminal branches were examined in the evergreen woody plant, Eurya japonica. The branch order number was determined centrifugally. The trunk was given order number 1; branches issuing directly from the trunk were order 2; branches growing on order 2 branches were order 3, and so on. The results of this study show the differential patterns of vegetative growth and reproduction in relation to the branch orders. Lower-order shoots of terminal branches grew more, but produced few flowers. On the other hand, for the higher-order terminal branches, shoot growth was very limited but flowering was more intense. The results show that a tree can be interpreted not as a mere population of equivalent modules but as a spatially structured population. Thus, it is essential to consider the position of modules within the branch system when patterns of vegetative growth and reproduction are examined. It is hypothesized that the difference in the opportunity cost in relation to the branch orders is the main cause of the spatial structure for patterns of vegetative growth and reproduction. Furthermore, for same-order terminal branches, current-year shoot elongation was independent of flowering intensity. These results suggest that this species only invests resources in reproduction that are surplus to its requirements for the functions associated with survival, such as growth and/or storage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004680050226
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  • 13
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray studies on the trypsin inhibitor I-2 from wheat germ and its complex with trypsin (1993)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 49 (1993), S. 594-596 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A Bowman–Birk type trypsin inhibitor I-2, Mr = 14 000, 123 amino-acid residues, isolated from wheat germ, and its complex with trypsin have been crystallized. For I-2 two morphologically different crystal forms were obtained. Crystal form 1 is tetragonal, P4122 or P4322, with a = 55.45 (2), c = 129.1 (2) Å and V = 3.97 (2) × 105 Å3. The crystals diffract X-rays very anisotropically, to less than 6 Å resolution normal to the c* direction, but up to 3 Å resolution in the other directions. Crystal form 2 is monoclinic, space group C2. The cell parameters show significant variation even for crystals in the same batch. The median parameters are: a = 83.9, b = 41.5, c = 45.7 Å, β = 95.9° and V = 1.58 × 105 Å3. The diffraction pattern is isotropic and reflections up to 2.2 Å resolution were observed. The crystals of the complex between bovine trypsin and I-2 (2:1) belong to the orthorhombic space group P212121 with a = 73.49 (2), b = 120.56 (3), c = 70.04 (2) Å and V = 6.206 (5) × 105 Å3. The crystals diffract up to 2.3 Å resolution, and contain one complex of 60 100 Da in an asymmetric unit.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444993006134
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  • 14
    Electronic Resource
    Electronic Resource
    Structure of a new alkaline serine protease (M-protease) from Bacillus sp. KSM-K16 (1995)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 199-206 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: An alkaline serine protease, M-protease, from Bacillus sp. KSM-K16 has been crystallized. Two morphologically different crystal forms were obtained. Crystal data of form 1: space group P212121, a = 47.3, b = 62.5, c = 75.6 Å, V = 2.23 × 105 Å3, Z = 4 and Vm = 2.09 Å3 Da−1. Crystal data of form 2: space group P212121, a = 75.82 (2), b = 57.79 (2), c = 54.19 (1) Å, V = 2.29 (2) × 105 Å3, Z = 4 and Vm = 2.15 Å3 Da−1. The crystal structure of M-protease in form 2 has been solved by molecular replacement using the atomic model of subtilisin Carlsberg (SBC) which is 60% homologous with M-protease, and refined to the crystallographic R-factor of 0.189 for 7004 reflections with Fo/σ(F) 〉 3 between 7 and 2.4 Å resolution. The final model of M-protease contains 1882 protein atoms, two calcium ions and 44 water molecules. The three-dimensional structure of M-protease is essentially similar to other subtilisins of known structure. The 269 Cα positions of M-protease have an r.m.s. difference of 1.06 Å with the corresponding positions of SBC. The crystal data of form 2 are close to those of SBC, though the structure determination of form 2 made it clear that it is not isomorphous to the crystal structure of SBC. The deletions of amino acids occur at the residues 36′ and 160′–163′ compared with SBC (numerals with primes show the numbering for SBC). The deletion of the four residues (160′–163′) may significantly affect the lack of isomorphism between M-protease and SBC.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994009960
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  • 15
    Electronic Resource
    Electronic Resource
    An Immunological Assessment of Myosin Degradation in Pressurized Chicken Muscle (2001)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 66 (2001), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : The factors affecting myosin degradation that occurred during aging following high-pressure treatment over a pressure range from 200 to 600 MPa were investigated by using SDS-PAGE and immunoblotting analysis. The immunoblot pattern of myosin in muscle stored at 37°C for 48 h after pressure treatment at 0. 1 MPa (atmospheric pressure) or 200 MPa for 5 min was similar to that of native myosin incubated with cathepsin D, whereas at 400 or 600 MPa the pattern was close to that of native myosin incubated with cathepsin B. This phenomenon was reflected in the pressure-susceptibilities of cathepsins B and D as reported in the literature (Homma and others 1994). However, these catheptic enzymes released by pressure treatment are unlikely to play a role in pressure-induced tenderization of meat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2001.tb16092.x
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  • 16
    Electronic Resource
    Electronic Resource
    Monitoring Myosin Degradation During Conditioning in Chicken Meat Using an Immunological Method (2001)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 66 (2001), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Changes of chicken breast myosin during storage at 2°C and 37°C were monitored immunochemically. Anti-myosin subfragment-1 (S-1) monoclonal antibody, which recognized epitopes within the 27 kDa fragment of S-1, and the anti-myosin rod polyclonal antiserum, were prepared. Myosin degradation products were not detected in muscle extracts stored for 3 weeks at 2°C. In contrast, storage at 37°C brought about the degradation of myosin heavy chain to immunologically detectable small fragments. While, myosin rod produced during the conditioning period was not decomposed into any small filaments. Namely, storage of muscle at 37°C resulted in minor amounts of myosin heavy chain degradation, with initial conversion to rod and S-1 fragments, and subsequent breakdown occurred in the S-1 region only. Immunoblot assay also suggested that the pattern of changes in myosin heavy chain in muscle incubated at 37°C was similar to that produced by in vitro digestion with cathepsin D.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2001.tb16091.x
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  • 17
    Electronic Resource
    Electronic Resource
    ERYTHROCYTE GLYCOSPHINGOLIPIDS OF FOUR SIBLINGS WITH THE RARE BLOOD GROUP p PHENOTYPE AND THEIR PARENTS (1981)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 8 (1981), S. 0 
    Details
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Erythrocytes that exhibit the rare blood group p phenotype lack the P antigen (globotetraosylceramide) and the Pk antigen (globotriaosylceramide). This phenotype is inherited as an autosomal recessive condition and the red cells of heterozygous individuals, parents and children of p persons, are serologically normal but no chemical analyses of their red cells have been reported. We have studied an unusual family in which all five children exhibit the p phenotype. In addition to the abnormalities described previously, the erythrocytes of four siblings had twice the normal concentration of lactotriaoslyceramide and lactoneotetraosylceramide. These cells also contained 3-5 times as much sialosyllactoneotetraosylceramide and up to a two-fold increase in GM3 ganglioside. The glycolipids of the parents' erythrocytes were normal. Electrophoretic analysis of the glycoproteins of the proposita's erythrocytes revealed no abnormalities, but her erythrocyte membranes contained approximately 35% less galactosamine than normal red cells. This abnormality resulted from a marked decrease in galactosamine that was soluble in chloroformmethanol. The lipid-extracted residue, which contained the glycoproteins, had a normal galactosamine content.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1744-313X.1981.tb00940.x
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  • 18
    Electronic Resource
    Electronic Resource
    Structures and Properties of Sago Starches with Low and High Viscosities on Amylography (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 54 (1989), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Both amyloses and amylopectins from sago starches with low (280 BU, low-v) and high (735 BU, high-v) viscosities on amylography differed in molecular structures. The low-v amylopectin (average chain length, c.I., 22) was a smaller molecule with a slightly higher amount of long chains than the high-v amylopectin (c.I., 22). The number-and weight-average degrees of polymerization of the low-v amylose were 2490 and 5090, respectively, which were half those of the high-v amylose. The low-v amylose had a lower molar fraction of branched molecules with a shorter inner chain length than the high-v amylose, but both branched molecules had a similar number (17–19) of chains on the average. Both starch granules had the same crystalline type (Ca) and amylose content (24%).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1989.tb08596.x
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  • 19
    Electronic Resource
    Electronic Resource
    Surface films of protein and a protein-lipopolysaccharide complex extracted from Pseudomonas aeruginosa
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 255 (1972), S. 734-743 
    Details
    ISSN: 0005-2736
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2736(72)90386-0
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  • 20
    Electronic Resource
    Electronic Resource
    Amino acid sequence of pheromone-biosynthesis-activating neuropeptide (PBAN) of the silkworm, Bombyx mori
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 163 (1989), S. 520-526 
    Details
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0006-291X(89)92168-2
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