title: A rainfall loading response recorded at 300 meters depth: implications for geological weighing lysimeters

authors: Sophocleous, Marios

subjects: pore water pressure

abstract: Static pore water pressures in confined aquifers vary in response to ground surface loading changes, including precipitation and evaporation. Under certain hydrogeological conditions such aquifers can function as giant natural weighing lysimeters, referenced here as ‘geological weighing lysimeters’. The extent of the land area ‘weighed’ increases with aquifer depth and it is of interest to establish at what depth it is still possible to monitor surface water budgets. An 86 mm rainfall event produced a clear loading signal in a well in western Kansas at 300 m depth. The loading effect is quantitatively consistent with elastic deformation induced by the rainfall mass and suggests that geological weighing lysimeters could operate at considerably greater depths, thereby monitoring water budgets over a significant land area.

text: A rainfall loading response recorded at 300 meters depth: implications for geological weighing lysimeters Static pore water pressures in confined aquifers vary in response to ground surface loading changes, including precipitation and evaporation. Under certain hydrogeological conditions such aquifers can function as giant natural weighing lysimeters, referenced here as ‘geological weighing lysimeters’. The extent of the land area ‘weighed’ increases with aquifer depth and it is of interest to establish at what depth it is still possible to monitor surface water budgets. An 86 mm rainfall event produced a clear loading signal in a well in western Kansas at 300 m depth. The loading effect is quantitatively consistent with elastic deformation induced by the rainfall mass and suggests that geological weighing lysimeters could operate at considerably greater depths, thereby monitoring water budgets over a significant land area.

year: 2006

title: Caldolase, a chelator-insensitive extracellular serine proteinase from a Thermus spp.

authors: Saravani, G.A.

subjects: biology

abstract: An extracellular alkaline serine proteinase from Thermus strain ToK3 was isolated and purified to homogeneity by (NH4)2SO4 precipitation followed by ion-exchange chromatography on DEAE-cellulose and QAE-Sephadex, affinity chromatography on N alpha-benzyloxycarbonyl-D-phenylalanyl-triethylenetetraminyl-Sepha rose 4B and gel-filtration chromatography on Sephadex G-75. The purified enzyme had a pI of 8.9 and an Mr determined by gel-permeation chromatography of 25,000. The specific activity was about 37,700 proteolytic units/mg with casein as substrate, and the pH optimum was 9.5. Proteolytic activity was inhibited by low concentrations of di-isopropyl phosphorofluoridate and phenylmethanesulphonyl fluoride, but was unaffected by EDTA, EGTA, o-phenanthroline, N-ethyl-5-phenylisoxazolium-3'-sulphonate, N alpha-p-tosyl-L-phenylalanylchloromethane, N alpha-p-tosyl-L-lysylchloromethane, trypsin inhibitors and pepstatin A. The enzyme contained approx. 10% carbohydrate and four disulphide bonds. No Ca2+, Zn2+ or free thiol groups were detected. It hydrolysed several native and dye-linked proteins and synthetic chromogenic peptides and esters. The enzyme was very thermostable (half-life values were 840 min at 80 degrees C, 45 min at 90 degrees C and 5 min at 100 degrees C). The enzyme was unstable at low ionic strength: after 60 min at 75 degrees C in 0.1 M-Tris/acetate buffer, pH 8, only 20% activity remained, compared with no loss in 0.1 M-Tris/acetate buffer, pH 8, containing 0.4 M-NaCl.

text: Caldolase, a chelator-insensitive extracellular serine proteinase from a Thermus spp. An extracellular alkaline serine proteinase from Thermus strain ToK3 was isolated and purified to homogeneity by (NH4)2SO4 precipitation followed by ion-exchange chromatography on DEAE-cellulose and QAE-Sephadex, affinity chromatography on N alpha-benzyloxycarbonyl-D-phenylalanyl-triethylenetetraminyl-Sepha rose 4B and gel-filtration chromatography on Sephadex G-75. The purified enzyme had a pI of 8.9 and an Mr determined by gel-permeation chromatography of 25,000. The specific activity was about 37,700 proteolytic units/mg with casein as substrate, and the pH optimum was 9.5. Proteolytic activity was inhibited by low concentrations of di-isopropyl phosphorofluoridate and phenylmethanesulphonyl fluoride, but was unaffected by EDTA, EGTA, o-phenanthroline, N-ethyl-5-phenylisoxazolium-3'-sulphonate, N alpha-p-tosyl-L-phenylalanylchloromethane, N alpha-p-tosyl-L-lysylchloromethane, trypsin inhibitors and pepstatin A. The enzyme contained approx. 10% carbohydrate and four disulphide bonds. No Ca2+, Zn2+ or free thiol groups were detected. It hydrolysed several native and dye-linked proteins and synthetic chromogenic peptides and esters. The enzyme was very thermostable (half-life values were 840 min at 80 degrees C, 45 min at 90 degrees C and 5 min at 100 degrees C). The enzyme was unstable at low ionic strength: after 60 min at 75 degrees C in 0.1 M-Tris/acetate buffer, pH 8, only 20% activity remained, compared with no loss in 0.1 M-Tris/acetate buffer, pH 8, containing 0.4 M-NaCl.

year: 1989

title: Kava and Maaori: New drug fashion or re-engagement with 'kawa'? [Invited presentation]

authors: Aporosa, S. 'Apo'

abstract: It is estimated there are more than 20,000 kava users in New Zealand on an average Friday or Saturday night, with increasing interest and uptake of this indigenous drink by Māori. This presentation argues that some of that increased use of kava by Māori can be interpreted as a cultural expression of pre-migration Hawaiki, rather than simply a new interaction with a foreign drug substance.

text: Kava and Maaori: New drug fashion or re-engagement with 'kawa'? [Invited presentation] It is estimated there are more than 20,000 kava users in New Zealand on an average Friday or Saturday night, with increasing interest and uptake of this indigenous drink by Māori. This presentation argues that some of that increased use of kava by Māori can be interpreted as a cultural expression of pre-migration Hawaiki, rather than simply a new interaction with a foreign drug substance.

year: 2016