403 research outputs found
TINJAUAN TENTANG TEKNIK DASAR TENDANGAN SABIT DALAM PENCAK SILAT PERSAUDARAAN SETIA HATI TERATE (PSHT) RANTING PENFUI TIMUR
Tendangan sabit merupakan tendangan berbentuk busur dan menggunakan punggung kaki pada perkenaannya dengan tumpuan satu kaki yang berputar sejauh 130Ā°. Tujuan penelitian ini untuk mengetahui teknik dasar tendangan sabit dalam Organisasi Pencak Silat Persaudaraan Setia Hati Terate (PSHT). Penelitian ini menggunakan metode kualitatif, dan dilakukan di Ranting Penfui Timur, teknik pengumpulan data yaitu observasi, wawancara dan dokumentasi, teknik analsis data menggunakan deskriptif kualitatif. Hasil tentang teknik dasar tendangan sabit dilakukan dengan langkah-langkah : 1. Pasang awal (kuda-kuda depan) dilakukan dengan posisi kaki kiri melangkah ke depan dan di tekuk, kedua tangan disilang untuk melindungi tubuh dan pandangan ke depan. 2. Persiapan serangan, dilakukan dengan kaki kanan diangkat dan kaki kiri dijinjit kemudian posisi badan diputar kira-kira 90o. 3. Serangan dilakukan dengan melepaskan tendangan kaki kanan dengan lintasan setengah lingkaran dan perkenaannya adalah punggung kaki. 4. Kembali ke sikap pasang awal. Kesimpulannya adalah latihan tendangan sabit sudah dilakukan dengan baik sesuai dengan tahapan-tahapannya.
 
Influences of the coating on silver nanoparticle toxicity in a chronic test with Daphnia magna
Uptake and localization of fluorescent labelled gold nanoparticles in living zebrafish (Danio rerio) using Light Sheet Microscopy
Transformation and distribution processes governing the fate and behaviour of nanomaterials in the environment: an overview
The Identity of Proteins Associated with a Small Heat Shock Protein during Heat Stress \u3ci\u3ein Vivo\u3c/i\u3e Indicates That These Chaperones Protect a Wide Range of Cellular Functions
The small heat shock proteins (sHSPs) are a ubiquitous
class of ATP-independent chaperones believed to
prevent irreversible protein aggregation and to facilitate
subsequent protein renaturation in cooperation
with ATP-dependent chaperones. Although sHSP chaperone
activity has been studied extensively in vitro, understanding
the mechanism of sHSP function requires
identification of proteins that are sHSP substrates in
vivo. We have used both immunoprecipitation and affinity
chromatography to recover 42 proteins that specifically
interact with Synechocystis Hsp16.6 in vivo during
heat treatment. These proteins can all be released from
Hsp16.6 by the ATP-dependent activity of DnaK and cochaperones
and are heat-labile. Thirteen of the putative
substrate proteins were identified by mass spectrometry
and reveal the potential for sHSPs to protect cellular
functions as diverse as transcription, translation, cell
signaling, and secondary metabolism. One of the putative
substrates, serine esterase, was purified and tested
directly for interaction with purified Hsp16.6. Hsp16.6
effectively formed soluble complexes with serine esterase
in a heat-dependent fashion, thereby preventing formation
of insoluble serine esterase aggregates. These
data offer critical insights into the characteristics of
native sHSP substrates and extend and provide in vivo
support for the chaperone model of sHSP function
The Identity of Proteins Associated with a Small Heat Shock Protein during Heat Stress \u3ci\u3ein Vivo\u3c/i\u3e Indicates That These Chaperones Protect a Wide Range of Cellular Functions
The small heat shock proteins (sHSPs) are a ubiquitous
class of ATP-independent chaperones believed to
prevent irreversible protein aggregation and to facilitate
subsequent protein renaturation in cooperation
with ATP-dependent chaperones. Although sHSP chaperone
activity has been studied extensively in vitro, understanding
the mechanism of sHSP function requires
identification of proteins that are sHSP substrates in
vivo. We have used both immunoprecipitation and affinity
chromatography to recover 42 proteins that specifically
interact with Synechocystis Hsp16.6 in vivo during
heat treatment. These proteins can all be released from
Hsp16.6 by the ATP-dependent activity of DnaK and cochaperones
and are heat-labile. Thirteen of the putative
substrate proteins were identified by mass spectrometry
and reveal the potential for sHSPs to protect cellular
functions as diverse as transcription, translation, cell
signaling, and secondary metabolism. One of the putative
substrates, serine esterase, was purified and tested
directly for interaction with purified Hsp16.6. Hsp16.6
effectively formed soluble complexes with serine esterase
in a heat-dependent fashion, thereby preventing formation
of insoluble serine esterase aggregates. These
data offer critical insights into the characteristics of
native sHSP substrates and extend and provide in vivo
support for the chaperone model of sHSP function
Uptake and depuration of gold nanoparticles in Daphnia magna
This study presents a series of short-term studies (total duration 48 h) of uptake and depuration of engineered nanoparticles (ENP) in neonate Daphnia magna. Gold nanoparticles (Au NP) were used to study the influence of size, stabilizing agent and feeding on uptake and depuration kinetics and animal body burdens. 10 and 30 nm Au NP with different stabilizing agents [citrate (CIT) and mercaptoundecanoic acid (MUDA)] were tested in concentrations around 0.5 mg Au/L. Fast initial uptake was observed for all studied Au NP, with CIT stabilized Au NP showing similar rates independent of size and MUDA showing increased uptake for the smaller Au NP (MUDA 10 nm > CIT 10 nm, 30 nm > MUDA 30 nm). However, upon transfer to clean media no clear trend on depuration rates was found in terms of stabilizing agent or size. Independent of stabilizing agent, 10 nm Au NP resulted in higher residual whole-animal body burdens after 24 h depuration than 30 nm Au NP with residual body burdens about one order of magnitude higher of animals exposed to 10 nm Au NP. The presence of food (P. subcapitata) did not significantly affect the body burden after 24 h of exposure, but depuration was increased. While food addition is not necessary to ensure D. magna survival in the presented short-term test design, the influence of food on uptake and depuration kinetics is essential to consider in long term studies of ENP where food addition is necessary. This study demonstrates the feasibility of a short-term test design to assess the uptake and depuration of ENP in D. magna. The findings underlines that the assumptions behind the traditional way of quantifying bioconcentration are not fulfilled when ENPs are studied.Peer reviewed: YesNRC publication: Ye
Redefining risk research priorities for nanomaterials
Chemical-based risk assessment underpins the current approach to responsible development of nanomaterials (NM). It is now recognised, however, that this process may take decades, leaving decision makers with little support in the near term. Despite this, current and near future research efforts are largely directed at establishing (eco)toxicological and exposure data for NM, and comparatively little research has been undertaken on tools or approaches that may facilitate near-term decisions, some of which we briefly outline in this analysis. We propose a reprioritisation of NM risk research efforts to redress this imbalance, including the development of more adaptive risk governance frameworks, alternative/complementary tools to risk assessment, and health and environment surveillance
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