エネルギー輸出国の脆弱性とエネルギーセキュリティの評価フレームワーク：現在の化石燃料依存社会と将来の水素社会の事例

京都大学新制・課程博士博士(エネルギー科学)甲第24924号エネ博第466号京都大学大学院エネルギー科学研究科エネルギー社会・環境科学専攻(主査)教授 MCLELLAN Benjamin, 教授 宇根﨑 博信, 教授 河本 晴雄学位規則第4条第1項該当Doctor of Energy ScienceKyoto UniversityDFA

Economics of interceptor drains : a case study

This case study determines the most likely rate of return to capital invested in constructing seepage interceptor drains to reduce the effect of waterlogging on crop and pasture yields. The analysis of a farm in the Denbarker region, west of Albany, determined what increases were needed in pasture growth to justify the cost of constructing drains across four adjacent paddocks. The benefits of changing rotations to include lupins were also determined, as growing lupins was unprofitable before the construction of drains

Deep tillage : keep an eye on costs as well as yields

Deep tillage overcomes compaction of sandy soils caused by movement of heavy machinery. Many experiments since 1981 have shown cereal yields improve as a result of deep tillage. However, the increased yield does not necessarily mean more profit when costs are taken into account. To determine the profitability of deep tillage farmers must consider its impact on other farm operations. A whole-farm analysis is needed to accurately determine the increase in profit resulting from deep tillag

Derivation of supply curves for catchment water effluents meeting specific salinity concentration targets in 2050: linking farm and catchment level models or “Footprints on future salt / water planes”

The salt burden in a stream reflects the blend of salty and fresh flows from different soil areas in its catchment. Depending not only on long-run rainfall, water yields from a soil are also determined by land cover: lowest if the area is forested and greatest if cleared. Water yields under agro-forestry, lucerne pasture, perennial grass pasture, and annual pasture or cropping options span the range of water yields between the extremes of forested and cleared lands. This study explores quantitative approaches for connecting the hydrologic and economic consequences of farm-level decisions on land cover (productive land uses) to the costs of attaining different catchment level targets of water volumes and salt reaching downstream users; environmental, agricultural, domestic, commercial and industrial. This connection is critical for the resolution of the externality dilemma of meeting downstream demands for water volume and quality. New technology, new products and new markets will expand options for salinity abatement measures in the dryland farming areas of watershed catchments. The development of appropriate policy solutions to address demands for water volumes and quality depends on the possibility of inducing targeted land use change in those catchments or parts of catchments where decreased saline flows or increased fresh water flows can return the best value for money. This study provides such a link.salinity, targets, opportunity cost, concentration, dilution, effluent, externality, supply, demand, policy, water quality, new technology, new markets, Resource /Energy Economics and Policy,

Mathematical optimisation of drainage and economic land use for target water and salt yields

Land managers in upper catchments are being asked to make expensive changes in land use, such as by planting trees, to attain environmental service targets, including reduced salt loads in rivers, to meet needs of downstream towns, farms and natural habitats. End-of-valley targets for salt loads have sometimes been set without a quantitative model of cause and effect regarding impacts on water yields, economic efficiency or distribution of costs and benefits among stakeholders. This paper presents a method for calculating a ‘menu’ of technically feasible options for changes from current to future mean water yields and salt loads from upstream catchments having local groundwater flow systems, and the land-use changes to attain each of these options at minimum cost. It sets the economic stage for upstream landholders to negotiate with downstream parties future water-yield and salt-load targets, on the basis of what it will cost to supply these ecosystem services.discounting, landuse, NPV, opportunity-cost, salinity, Resource /Energy Economics and Policy,

Land use planning for agriculture and sustainable rural development

An important goel for agriculture will be to achieve sustainable land use patterns and management systems. Land use planning has a role to play in helping agticulture achieve this goal. Ian Kininmouth, Andrew Bathgate, Ross George and Dennis Van Gool discuss the directions land use planning could follow

Relaxin family peptide receptors in GtoPdb v.2021.3

Relaxin family peptide receptors (RXFP, nomenclature as agreed by the NC-IUPHAR Subcommittee on Relaxin family peptide receptors [18, 81]) may be divided into two pairs, RXFP1/2 and RXFP3/4. Endogenous agonists at these receptors are heterodimeric peptide hormones structurally related to insulin: relaxin-1, relaxin, relaxin-3 (also known as INSL7), insulin-like peptide 3 (INSL3) and INSL5. Species homologues of relaxin have distinct pharmacology and relaxin interacts with RXFP1, RXFP2 and RXFP3, whereas mouse and rat relaxin selectively bind to and activate RXFP1 [184]. relaxin-3 is the ligand for RXFP3 but it also binds to RXFP1 and RXFP4 and has differential affinity for RXFP2 between species [183]. INSL5 is the ligand for RXFP4 but is a weak antagonist of RXFP3. relaxin and INSL3 have multiple complex binding interactions with RXFP1 [189] and RXFP2 [91] which direct the N-terminal LDLa modules of the receptors together with a linker domain to act as a tethered ligand to direct receptor signaling [186]. INSL5 and relaxin-3 interact with their receptors using distinct residues in their B-chains for binding, and activation, respectively [225, 104]

Relaxin family peptide receptors (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

Relaxin family peptide receptors (RXFP, nomenclature as agreed by the NC-IUPHAR Subcommittee on Relaxin family peptide receptors [18, 75]) may be divided into two pairs, RXFP1/2 and RXFP3/4. Endogenous agonists at these receptors are heterodimeric peptide hormones structurally related to insulin: relaxin-1, relaxin, relaxin-3 (also known as INSL7), insulin-like peptide 3 (INSL3) and INSL5. Species homologues of relaxin have distinct pharmacology and relaxin interacts with RXFP1, RXFP2 and RXFP3, whereas mouse and rat relaxin selectively bind to and activate RXFP1 [172]. relaxin-3 is the ligand for RXFP3 but it also binds to RXFP1 and RXFP4 and has differential affinity for RXFP2 between species [170]. INSL5 is the ligand for RXFP4 but is a weak antagonist of RXFP3. relaxin and INSL3 have multiple complex binding interactions with RXFP1 [176] and RXFP2 [84] which direct the N-terminal LDLa modules of the receptors together with a linker domain to act as a tethered ligand to direct receptor signaling [173]. INSL5 and relaxin-3 interact with their receptors using distinct residues in their B-chains for binding, and activation, respectively [211, 97]

Relaxin family peptide receptors in GtoPdb v.2023.1

Relaxin family peptide receptors (RXFP, nomenclature as agreed by the NC-IUPHAR Subcommittee on Relaxin family peptide receptors [23, 119]) may be divided into two pairs, RXFP1/2 and RXFP3/4. Endogenous agonists at these receptors are heterodimeric peptide hormones structurally related to insulin: relaxin-1, relaxin, relaxin-3 (also known as INSL7), insulin-like peptide 3 (INSL3) and INSL5. Species homologues of relaxin have distinct pharmacology and relaxin interacts with RXFP1, RXFP2 and RXFP3, whereas mouse and rat relaxin selectively bind to and activate RXFP1 [260]. relaxin-3 is the ligand for RXFP3 but it also binds to RXFP1 and RXFP4 and has differential affinity for RXFP2 between species [259]. INSL5 is the ligand for RXFP4 but is a weak antagonist of RXFP3. relaxin and INSL3 have multiple complex binding interactions with RXFP1 [267] and RXFP2 [132] which direct the N-terminal LDLa modules of the receptors together with a linker domain to act as a tethered ligand to direct receptor signaling [262]. INSL5 and relaxin-3 interact with their receptors using distinct residues in their B-chains for binding, and activation, respectively [321, 152]