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  • 1
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    In:  Blumea - Biodiversity, Evolution and Biogeography of Plants (0006-5196) vol.56 (2011) nr.1 p.21
    Publication Date: 2015-03-06
    Description: Selaginella devolii sp. nov. is described from four populations located in central and southern Taiwan. It is an annual prostrate lycophyte, growing on moist rocky slopes. Its diagnostic characteristics include its small size, tiny broadly ovate trophophylls, complanate strobili, and sporangia which are only formed at the ventral sporophylls. Notes on taxonomy and distribution and a line illustration are provided.
    Keywords: IUCN Red List ; Selaginella devolii ; Selaginellaceae ; Taiwan ; taxonomy
    Repository Name: National Museum of Natural History, Netherlands
    Type: Article / Letter to the editor
    Format: application/pdf
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  • 2
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    Unknown
    In:  Blumea: Biodiversity, Evolution and Biogeography of Plants vol. 56 no. 1, pp. 21-23
    Publication Date: 2024-01-12
    Description: Selaginella devolii sp. nov. is described from four populations located in central and southern Taiwan. It is an annual prostrate lycophyte, growing on moist rocky slopes. Its diagnostic characteristics include its small size, tiny broadly ovate trophophylls, complanate strobili, and sporangia which are only formed at the ventral sporophylls.\nNotes on taxonomy and distribution and a line illustration are provided.
    Keywords: IUCN Red List ; Selaginella devolii ; Selaginellaceae ; Taiwan ; taxonomy
    Repository Name: National Museum of Natural History, Netherlands
    Type: info:eu-repo/semantics/article
    Format: application/pdf
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  • 3
    ISSN: 1432-1424
    Keywords: Calcium-activated potassium channel ; Cholesterol ; Conductance ; Lateral elastic stress ; Lipid bilayers ; Lipid-channel interactions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The ubiquity of cholesterol in cell membranes and changes in its concentration during development, aging and in various diseases suggest that it plays an important role in modulating cell function. We examined this possibility by monitoring the effects of cholesterol on the activity of the calcium-activated potassium (BK) channel reconstituted into lipid bilayers from rat brain homogenates. Increasing the cholesterol concentration to 11% of total lipid weight resulted in a 70% reduction in channel mean open time and a reduction of the open probability of the channel by 80%. Channel conductance was reduced by 7%. Cholesterol is known to change the order state and the modulus of compressibility of bilayers. These physico-chemical changes may be translated into an overall increase in the structural stress in the bilayer, and this force may be transmitted to proteins residing therein. By examining the characteristics of the BK channel as a function of temperature, in the presence and absence of cholesterol, we were able to estimate the activation energy based on Arrhenius plots of channel kinetics. Cholesterol reduced the activation energy of the BK channel by 50% for the open to closed transition. This result is consistent with an increased stress energy in the bilayer and favors the channel moving into the closed state. Taken together, these data are consistent with a model in which cholesterol induces structural stress which enhances the transition from the open to the closed state of the channel. We suggest that this is an important mechanism for regulating the activity of membrane-integral proteins and therefore membrane function, and that the concept of structural stress may be relevant to understanding the modulation of ion channel activity in cell membranes.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-1424
    Keywords: Lipid-protein interactions ; Elastic stress ; Curvature stress ; Reconstituted potassium channel
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We have recently shown (Chang et al., 1995) that lipid-channel interactions, exemplified by the effects of cholesterol on the calcium-activated potassium (BK) channel, profoundly affect channel properties. The present study further explores such interactions by monitoring changes in BK channel behavior after reconstitution into bilayers where the size of phospholipid (PL) headgroups is increased and where the freedom of motion (inverse order) of fatty acid chains is incremented. Increasing the PL headgroup cross-sectional area, from that of N-meth-DOPE to that of DOPC (an increase from ca. 60 to 70 Å2), is associated with a doubling of the channel mean opentime. Channel conductance, however, was unaffected. Increasing the order of the fatty acid chains, from that of DOPE to POPE and to that of DEPE, had no significant effect on channel properties (at 22°C). We interpret the changes reported here to reflect lipid-protein interactions through the induction of structural stress related to the headgroup structures of phospholipids.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 67 (2002), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Hens were intramuscularly (im) immunized on thighs by using urease (E.C. 3.5.1.5) from Helicobactor pylori as antigen. The specificity of IgY against urease of H. pylori increased gradually after initial immunization. The collected yolk was microencapsulated with 10% or 20%β-cyclodextrin (β-CD) and gum arabic by a spray-drier. Microencapsulation was effective in protecting the IgY activity against pepsin. Liposome prepared at the lecithin/ cholesterol ratio of 1/0.25 (mole/mole) displayed satisfactory encapsulation efficiency (69%) of IgY. Increase in cholesterol content in the liposomal structure exhibited a stronger protection effect of IgY against pepsin and acid.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 67 (2002), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Citrus and jelly fig achene pectinesterase (PE) (1 U/mL) activity was remarkably inhibited by PE inhibitor (PEI) (2 mg/mL) from jelly fig (Ficus awkeotsang Makino) achenes, in the absence or presence of 0- to 500-mM salts or 0 to 30% of sugars. Changes in temperature (20 to 40 °C) apparently decreased the activity of citrus PE in PE-PEI reaction mixture. Enzyme-activity curves for jelly fig PE alone and for that in combination with PEI were parallel. Activity of crude PEs (1 U/mL) from tomato, apple, asparagus, and guava was reduced remarkably. Cloud loss of fresh tomato juice, apple juice, and papaya juice was greatly inhibited by PEI (1 mg/mL) during 12-wk storage.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 66 (2001), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Albumen from hen eggs was diluted 3-fold with 0.05 M NaCl solution at pH 4.0 and was further treated with 30% ethanol for 8 h. The supernatant (77900 U/mg protein) thus obtained was further diluted (2.5-fold) with distilled water and its pH value was adjusted to 8.0 before being subjected to alcohol-insoluble cross-linked pea pod solid (AICLPPS) ion-exchange chromatography for lysozyme isolation. Results showed that AI-CLPPS ion-exchange chromatography increased the purification to 68-fold with a 72% lysozyme recovery from the starting albumen.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 66 (2001), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Pectinesterase (PE) was isolated from jelly fig (Ficus awkeotsang Makino) achenes, then the optimal conditions for de-esterification and transacylation reactions were determined. Molecular weight of pectin (DE = 62.8 %) when reacted with PE at pH 6.5 and 45 °C in 0.2 M NaCl for 20 min remarkably increased from the original 72 kDa to 410 kDa, as determined by Fractogel TSK 65(S) gel permeation chromatography. Prolonging the incubation time of pectin-PE mixtures to 2 and 4 h also increased the molecular weights of pectin. Therefore, transacylation reaction was considered to occur and to increase the molecular weight of pectins when de-esterification reaction was catalyzed by pectinesterase (PE).
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 67 (2002), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Lactoferrin (LF) in colostral whey was isolated by anti-LF immunoglobulin in yolk (IgY)-Sepharose 4B immunoaffinity chromatography, and parameters such as binding capacity (qm) and dissociation constant (Kd, × 10−6 M) of this immunoaffinity gel for LF were discussed. Purification folds for colostral whey I (from colostrum collected within 6 d of postpartum) and colostral whey II (from colostrum collected within 1 d of postpartum) by anti-LF IgY-immunoaffinity chromatography were 135.80 and 103.60, respectively. The recovery for LF in the same colostral whey sample by anti-LF IgY-immunoaffinity chromatography was 82 to 99 %. qm of anti-LF IgY-immunoaffinity gel for LF in colostral whey I and whey II were 0.372 and 0.272 mg LF/mL wet gel, respectively. Kd of anti-LF IgY-immunoaffinity gel for LF in colostral whey I was 1.594 × 10−6 M and II was 1.587 × 10−6 M.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 65 (2000), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: D and z values and some thermodynamic parameters of immunoglobulin G (IgG) in phosphate buffer solution (PBS) (0.15 M NaCl/0.01 M phosphate buffer, pH 7.0) and colostral whey, with or without the presence of thermal protectants, were calculated in model systems. The D and z values for separated IgG in PBS were much lower than those for separated IgG in 20% glycerol, whey, and whey with 20% glycerol. IgG in colostral whey showed larger D and z values with the protectants. The heat denaturing rate constants at 70-82°C for separated IgG in PBS were larger than those of IgG in colostral whey; and the energies of activation for separated IgG in PBS, 0.2% glutamic acid, 10% whole milk, 20% maltose and 20% glycerol were also larger.
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