22 research outputs found

    The influence of money stock growth changes on interest rates, 1981

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    Milton Friedman's theory of the influence of money stock changes on interest rates states that a change in the money stock will produce three different effects on interest rates. They are the liquidity effect, the income effect and the price anticipations effect. This study attempts to investigate the hypothesis that the effect on interest rates of changes in money stock growth depends on whether people are or are not inflenced by inflationary price expectations. To investigate this hypothesis we use a lagged modle relating interest rates to lagged money stock growth variables. Using United States' data the empirical results are consistent with our hypothesis that the effect on interest rates of changes in money stock growth does depend on whether people are or are not influenced by inflationary price expectations. Our study is also cosistent with Milton Friedman's theory of the influence of money stock growth on interest rates: an increase in money stock will produce the liquidity effect, the income effect and the price anticipations effect on interest rates

    แรงจูงใจและความผูกพันต่อองค์การของบุคลากรสานักพัฒนา อุตสาหกรรมสนับสนุน กรมส่งเสริมอุตสาหกรรม

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    การค้นคว้าอิสระ (บธ.ม.) -- มหาวิทยาลัยเทคโนโลยีราชมงคลพระนคร, 2559The purpose of this research was to investigate the motivation of the personnel working in the Bureau of Supporting Industries Development, Department of Industrial Promotion, and to study the organizational commitment and the relationship between work motivations. The sample used in this study consisted of 59 personnel in the Bureau of Supporting Industries Development, Department of Industrial Promotion. The author used Quantitative Approach by survey method using data collection by questionnaires. The collected data were analyzed by using the parameters: Percentage, μ, σ, and . When analyzing data from the questionnaires, it was found that most of respondents' data was male. The age range was 51 years and over. They were mostly government officials, most of whom had more than 26 years of work experience. Their salary ranged from 15,001 to 20,000 baht, and most of them were motivated by motivation factors in a high level. The motivation for supporting factors was moderate. The respondents' organizational commitment variables were at a high level. When testing the motivation variables, it was found that the variables that positively correlated with organizational commitment were job characteristics, job responsibilities, career path in Policy and Administration, salaries and benefits, interpersonal relationship, and working environment.Rajamangala University of Technology Phra Nakho

    Characterization of a novel binding protein for Fortilin/TCTP--component of a defense mechanism against viral infection in Penaeus monodon.

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    The Fortilin (also known as TCTP) in Penaeus monodon (PmFortilin) and Fortilin Binding Protein 1 (FBP1) have recently been shown to interact and to offer protection against the widespread White Spot Syndrome Virus infection. However, the mechanism is yet unknown. We investigated this interaction in detail by a number of in silico and in vitro analyses, including prediction of a binding site between PmFortilin/FBP1 and docking simulations. The basis of the modeling analyses was well-conserved PmFortilin orthologs, containing a Ca(2+)-binding domain at residues 76-110 representing a section of the helical domain, the translationally controlled tumor protein signature 1 and 2 (TCTP_1, TCTP_2) at residues 45-55 and 123-145, respectively. We found the pairs Cys59 and Cys76 formed a disulfide bond in the C-terminus of FBP1, which is a common structural feature in many exported proteins and the "x-G-K-K" pattern of the amidation site at the end of the C-terminus. This coincided with our previous work, where we found the "x-P-P-x" patterns of an antiviral peptide also to be located in the C-terminus of FBP1. The combined bioinformatics and in vitro results indicate that FBP1 is a transmembrane protein and FBP1 interact with N-terminal region of PmFortilin

    beta-Thymosins and Hemocyte Homeostasis in a Crustacean

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    Thymosin proteins are well known for their actin-binding activity. Thymosin beta 4 (T beta 4) has been associated with biological activities in tissue repair and cell migration via interaction with ATP-synthase in vertebrates, while the information of similar thymosin functions in invertebrates is limited. We have shown previously that ATP-synthase is present on the surface of crayfish hematopoietic tissue (HPT) cells, and that astakine 1 (Ast1, an invertebrate cytokine) was found to interact with this beta-subunit of ATP synthase. Here, we identified five different beta-thymosins from Pacifastacus leniusculus, designated Pl-beta-thymosin1-5. The two dominant isoforms in brain, HPT and hemocytes, Pl-beta-thymosin1 and 2, were chosen for functional studies. Both isoforms could bind to the b-subunit of ATP-synthase, and Pl-beta-thymosin1, but not Pl-beta-thymosin2, significantly increased extracellular ATP formation. Moreover, Pl-beta-thymosin1 stimulated HPT cell migration in vitro and Ast1 blocked this effect. Pl-beta-thymosin2 increased the circulating hemocyte number at an early stage after injection. Additionally, in vivo injection of Pl-beta-thymosin1 resulted in significant reduction of reactive oxygen species (ROS) production in crayfish HPT whereas Pl-beta-thymosin2 had a similar but transient effect. Both Pl-beta-thymosins induced the expression of Ast1 and superoxide dismutase (SOD) transcripts, while silencing of endogenous Pl-beta-thymosin 1 and 2 by RNAi resulted in significant reduction of the Ast1 and SOD transcripts. The diverse effects exhibited by Pl-beta-thymosin1 and Pl-beta-thymosin2 indicates that these proteins are involved in a complex interaction that regulates the hematopoietic stem cell proliferation and differentiation

    The predicted 3-D model and functional mapping of Fortilin from <i>Penaeus monodon</i>.

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    <p>(A) The predicted structure model of <i>Pm</i>Fortilin contains six beta hairpins, eleven strands and three helices: The helical domain (helix-helix interaction) along the residues 77–126 and a flexible loop at residues 38–62. (B) A graphical representation of the functional mapping of <i>Pm</i>Fortilin protein, was analyzed by SMART and the Motif Scan server. The following elements are shown: TCTP signatures at residues 45–55 on the flexible loop and 123–145 on the C-terminal, Ca<sup>2+</sup>-binding domain at residues 76–110 and DNA binding domain at residues 80–81, 83–84 and 88 also on the helical domains, serine phosphorylation sites at the residues 50, 62 and 64, threonine phosphorylation sites at the residues 17, 60 and 103, tyrosine phosphorylation sites at the residues 18, 20, 28 and 92. The ten amino acid residues at the N-terminal show high conservation with the protein transduction domains (PTDs) and may allow trans-membrane transport.</p

    Transmembrane localization of FBP1-GFP in Sf9 cell.

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    <p>The cellular localization of FBP1-GFP expressed in Sf9 cell was observed using confocal laser scanning microscopy at 48 h post-transfection. The plasma membrane was stained with DiI (Invitrogen) and shows co-localization of both fluorescent (green for GFP and red for DiI) after merging. Bright field is shown in the last panel. The scale bars indicate 10 µm.</p

    Molecular interaction models of <i>Pm</i>Fortilin/FBP1.

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    <p>(A top) A space-filling model representing the combination of two possible interactions of FBP1 (grey), at the opposite sides of <i>Pm</i>Fortilin (blue). (A bottom) A cartoon of the space-filling model showing the two conformations, A and B and the binding of <i>Pm</i>Fortilin to the C-terminus of FBP1. The predictions were performed with four separate modes: Balance, Electrostatic, Hydrophobic and VdW+Elec mode. (B–E) The lowest energy conformations of each of the four docking modes. The <i>Pm</i>Fortilin molecule (blue) and FBP1 (pink, yellow, magenta and green).</p

    The yeast two–hybrid assay.

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    <p>The yeast two-hybrid interaction between <i>Pm</i>Fortilin fragments and FBP1 in <i>S.cerevisiae</i> AH109 cells. (A)YPDA control to show yeast growth. (B) β-galactosidase activity of the yeast cultures in selective medium determined by a colony-lift filter assay.</p
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