title: Greater understanding of spacing needs for children’s eye movements during on-screen reading is required

authors: Vanderschantz, Nicholas

subjects: computer science

abstract: This paper endeavors to consolidate current knowledge and empirical research concerning the use of typography for children’s on-screen reading. This paper is not intended as a full literature review, but attempts to raise awareness of the areas required for future investigation. This evaluation indicates a significant gap in the literature of children’s on-screen reading and proposes a need for further investigations in typographical spacing. These future studies need to objectively consider children’s eye movements and the effect of screen based text presentation on children’s comprehension.

text: Greater understanding of spacing needs for children’s eye movements during on-screen reading is required This paper endeavors to consolidate current knowledge and empirical research concerning the use of typography for children’s on-screen reading. This paper is not intended as a full literature review, but attempts to raise awareness of the areas required for future investigation. This evaluation indicates a significant gap in the literature of children’s on-screen reading and proposes a need for further investigations in typographical spacing. These future studies need to objectively consider children’s eye movements and the effect of screen based text presentation on children’s comprehension.

year: 2009

title: Screening of strains identified as extremely thermophilic bacilli for extracellular proteolytic activity and general properties of the proteinases from two of the strains

authors: Coolbear, C.

subjects: L-Arginine amidinohydrolase

abstract: A thermostable arginase (l-arginine amidinohydrolase, EC 3.5.3.1) was purified from the extreme thermophile ‘Bacillus caldovelox’ (DSM 411) by a procedure including DEAE-Sepharose chromatography, and gel filtration, anion exchange and hydrophobic-interaction fast-protein liquid chromatography, with substantial retention of the metal ion cofactor. The purified enzyme is a hexamer with a subunit Mr of 31000 ± 2000 and contains ≥1 Mn atom per subunit. Maximum activation on incubation with Mn²⁺ is 29%. Activity is optimal at pH 9 and at 60°C the Km for arginine is 3.4 mM and Ki(ornithine) is 0.55 mM. Incubation in 0.1 M Mops/NaOH buffer (pH 7) causes rapid inactivation at 60°C (t1/2(half life) = 4.5 min) and individually 0.1 mM Mn²⁺ or 1 mg/ml BSA (bovine serum albumin) increase the t1/2 of arginase activity 4-fold, but combined they produce > 1000-fold increase and a t1/2 = 105 min at 95°C. Aspartic acid and other species that bind Mn²⁺ can replace BSA, and it is suggested that arginase can be activated by free Mn²⁺. A strong chelating agent causes inactivation without subunit dissociation, but arginase dissociates rapidly at pH 2.5. Reassociation occurs at pH 9 and is unusual in that it does not require Mn²⁺.

text: Screening of strains identified as extremely thermophilic bacilli for extracellular proteolytic activity and general properties of the proteinases from two of the strains A thermostable arginase (l-arginine amidinohydrolase, EC 3.5.3.1) was purified from the extreme thermophile ‘Bacillus caldovelox’ (DSM 411) by a procedure including DEAE-Sepharose chromatography, and gel filtration, anion exchange and hydrophobic-interaction fast-protein liquid chromatography, with substantial retention of the metal ion cofactor. The purified enzyme is a hexamer with a subunit Mr of 31000 ± 2000 and contains ≥1 Mn atom per subunit. Maximum activation on incubation with Mn²⁺ is 29%. Activity is optimal at pH 9 and at 60°C the Km for arginine is 3.4 mM and Ki(ornithine) is 0.55 mM. Incubation in 0.1 M Mops/NaOH buffer (pH 7) causes rapid inactivation at 60°C (t1/2(half life) = 4.5 min) and individually 0.1 mM Mn²⁺ or 1 mg/ml BSA (bovine serum albumin) increase the t1/2 of arginase activity 4-fold, but combined they produce > 1000-fold increase and a t1/2 = 105 min at 95°C. Aspartic acid and other species that bind Mn²⁺ can replace BSA, and it is suggested that arginase can be activated by free Mn²⁺. A strong chelating agent causes inactivation without subunit dissociation, but arginase dissociates rapidly at pH 2.5. Reassociation occurs at pH 9 and is unusual in that it does not require Mn²⁺.

year: 1991

title: Ko te Korokoro o te Parata: Ko tātou tonu

authors: Higgins, Rawinia

subjects: Whakaora reo

abstract: I roto i ngā kaupapa whakaora i te reo Māori kei te waipukehia tātou e te reo Pākehā. Ahakoa he aha te kaupapa kei te mate tonu te reo Māori, ā kāore anō tātou kia kite kei hea te ara tika hei karo atu i te korokoro o te parata. Kāore hoki tātou e titiro me pēhea e whakarekareka ai te reo ki te huhua o ngā Māori, tuatahi; tuarua ki te motu whānui. Ko te āhua nei ko tātou tonu kei te patu i tō tātou reo. He tere nō tātou ki te whakahāwea i ngā tūmomo kaupapa whakaora reo Māori. Kei ngā ngutu noa iho te mate nui ki te reo Māori. Ka ara mai he kaupapa whakaora reo, arā kē te tokomaha o ngā tāngata e patu ana i taua kaupapa. Ahakoa ko wai, kāore tētahi kaupapa e noho tapu ana. Katoa kei te tātāhia e tātou tonu. Nō reira, me aha? Me tuku kia mate? Me pēhea te patu i te korokoro o te parata mehemea ko tātou tonu taua taniwha?

text: Ko te Korokoro o te Parata: Ko tātou tonu I roto i ngā kaupapa whakaora i te reo Māori kei te waipukehia tātou e te reo Pākehā. Ahakoa he aha te kaupapa kei te mate tonu te reo Māori, ā kāore anō tātou kia kite kei hea te ara tika hei karo atu i te korokoro o te parata. Kāore hoki tātou e titiro me pēhea e whakarekareka ai te reo ki te huhua o ngā Māori, tuatahi; tuarua ki te motu whānui. Ko te āhua nei ko tātou tonu kei te patu i tō tātou reo. He tere nō tātou ki te whakahāwea i ngā tūmomo kaupapa whakaora reo Māori. Kei ngā ngutu noa iho te mate nui ki te reo Māori. Ka ara mai he kaupapa whakaora reo, arā kē te tokomaha o ngā tāngata e patu ana i taua kaupapa. Ahakoa ko wai, kāore tētahi kaupapa e noho tapu ana. Katoa kei te tātāhia e tātou tonu. Nō reira, me aha? Me tuku kia mate? Me pēhea te patu i te korokoro o te parata mehemea ko tātou tonu taua taniwha?

year: 2011-04