title: Threads and emerging patterns: some recent developments in New Zealand music

authors: Lodge, Martin

abstract: Since 1984 there has been a deliberate and rapid internationalisation of New Zealand's business and financial position. This change in political attitude has also wrought major social and cultural changes. In music, the divergent philosophical pulls of ideas such as internationalism, postcolonialism, postmodernism, commercialisation and 'world music' have generated a changed atmosphere for composers, performers and audiences. The demise of the musical avant-garde has allowed a successful renegotiation of communication between professional musicians and listeners.

text: Threads and emerging patterns: some recent developments in New Zealand music Since 1984 there has been a deliberate and rapid internationalisation of New Zealand's business and financial position. This change in political attitude has also wrought major social and cultural changes. In music, the divergent philosophical pulls of ideas such as internationalism, postcolonialism, postmodernism, commercialisation and 'world music' have generated a changed atmosphere for composers, performers and audiences. The demise of the musical avant-garde has allowed a successful renegotiation of communication between professional musicians and listeners.

year: 1998

title: Purification and characterization of Ak.1 protease, a thermostable subtilisin with a disulphide bond in the substrate-binding cleft

authors: Toogood, Helen S.

subjects: calcium binding

abstract: Ak.1 protease, a thermostable subtilisin isolated originally from Bacillus st. Ak.1, was purified to homogeneity from the Escherichia coli clone PB5517. It is active against substrates containing neutral or hydrophobic branched-chain amino acids at the P₁ site, such as valine, alanine or phenylalanine. The Km and kcat of the enzyme decrease with decreasing temperature, though not to the same degree with all substrates, suggesting that specificity changes with temperature. The protease is markedly stabilized by Ca²⁺ ions. At 70 °C, a 10-fold increase in Ca²⁺ concentration increases the half-life by three orders of magnitude. Ak.1 protease is stabilized by Ca²⁺ to a greater extent than is thermitase. This may be due, in part, to the presence of an extra Ca²⁺-binding site in Ak.1 protease. Other metal ions, such as Sr²⁺, increase the thermostability of the enzyme, but to a significantly lower degree than does Ca²⁺. The structure of the protease showed the presence of a disulphide bond located within the active-site cleft. This bond influences both enzyme activity and thermostability. The disulphide bond appears to have a dual role: maintaining the integrity of the substrate-binding cleft and increasing the thermostability of the protease. The protease was originally investigated to determine its usefulness in the clean-up of DNA at high temperatures. However, it was found that this protease has a limited substrate specificity, so this application was not explored further.

text: Purification and characterization of Ak.1 protease, a thermostable subtilisin with a disulphide bond in the substrate-binding cleft Ak.1 protease, a thermostable subtilisin isolated originally from Bacillus st. Ak.1, was purified to homogeneity from the Escherichia coli clone PB5517. It is active against substrates containing neutral or hydrophobic branched-chain amino acids at the P₁ site, such as valine, alanine or phenylalanine. The Km and kcat of the enzyme decrease with decreasing temperature, though not to the same degree with all substrates, suggesting that specificity changes with temperature. The protease is markedly stabilized by Ca²⁺ ions. At 70 °C, a 10-fold increase in Ca²⁺ concentration increases the half-life by three orders of magnitude. Ak.1 protease is stabilized by Ca²⁺ to a greater extent than is thermitase. This may be due, in part, to the presence of an extra Ca²⁺-binding site in Ak.1 protease. Other metal ions, such as Sr²⁺, increase the thermostability of the enzyme, but to a significantly lower degree than does Ca²⁺. The structure of the protease showed the presence of a disulphide bond located within the active-site cleft. This bond influences both enzyme activity and thermostability. The disulphide bond appears to have a dual role: maintaining the integrity of the substrate-binding cleft and increasing the thermostability of the protease. The protease was originally investigated to determine its usefulness in the clean-up of DNA at high temperatures. However, it was found that this protease has a limited substrate specificity, so this application was not explored further.

year: 2000

title: Ngā takenga o te riri

authors: Murphy, Ēnoka

subjects: Pakanga

abstract: Ko te kaupapa ake o tēnei tuhinga, ko te whakawhāriki i ētahi kōrero mō te takenga mai o te riri, o te pakanga ki tā rā ngā kōrero a te Māori. Ko aua take mai rā kei ngā kōrero o tua whakarere, e hokia ana ki a Ranginui rāua ko Papatūānuku me tā rāua hūnuku. Ko tāna e pātai ake nei, nō hea ake te riri Māori, otirā, te pakanga a te Māori? Nō hea anō hoki āna tikanga? He aha ā ērā kōrero tauiratanga mai ki te toa o te Māori ki te whawhai. Ka mutu, ko te wāhi uaua pea o ngā pātai nei, ko te āhua ki ngā kōrero a te Māori kāore nei i te tapatahi mō te oroko hīmatanga. Ahakoa rā, tērā ōna rite, ōna rerekē. Kua tuhia nuitia te kaupapa o te oroko tīmatanga mai o te ao e ngā momo o te kaituhi Pākehā, ā, tērā anō hoki ko ngā tuhinga a te Māori ake. Inā te rerekē o ngā kōrero mō te oroko hīmatanga mai o te ao, tērā noa ētahi kōrero kua tīkina hei mātaitanga mō tēnei rangahau, mō tēnei tuhinga. Ka mutu, ko tā tēnei tuhinga, he whakaatu i te takenga mai o te riri, o te matawhāura Māori.

text: Ngā takenga o te riri Ko te kaupapa ake o tēnei tuhinga, ko te whakawhāriki i ētahi kōrero mō te takenga mai o te riri, o te pakanga ki tā rā ngā kōrero a te Māori. Ko aua take mai rā kei ngā kōrero o tua whakarere, e hokia ana ki a Ranginui rāua ko Papatūānuku me tā rāua hūnuku. Ko tāna e pātai ake nei, nō hea ake te riri Māori, otirā, te pakanga a te Māori? Nō hea anō hoki āna tikanga? He aha ā ērā kōrero tauiratanga mai ki te toa o te Māori ki te whawhai. Ka mutu, ko te wāhi uaua pea o ngā pātai nei, ko te āhua ki ngā kōrero a te Māori kāore nei i te tapatahi mō te oroko hīmatanga. Ahakoa rā, tērā ōna rite, ōna rerekē. Kua tuhia nuitia te kaupapa o te oroko tīmatanga mai o te ao e ngā momo o te kaituhi Pākehā, ā, tērā anō hoki ko ngā tuhinga a te Māori ake. Inā te rerekē o ngā kōrero mō te oroko hīmatanga mai o te ao, tērā noa ētahi kōrero kua tīkina hei mātaitanga mō tēnei rangahau, mō tēnei tuhinga. Ka mutu, ko tā tēnei tuhinga, he whakaatu i te takenga mai o te riri, o te matawhāura Māori.

year: 2017