Sistem Kontrol Kekeruhan dan Temperatur Air Laut Menggunakan Microcontroller Arduino Mega

Sistem kontrol merupakan bagian yang tidak dapat dipisahkan dalam kehidupan sehari-hari.. Saat ini penerapan sistem kontrol telah menjamah bidang perkebunan, perikanan ataupun pertanian. Dalam penelitian ini, sistem kontrol akan diterapkan pada proses budidaya perikanan seperti budidaya ikan kerapu. Dimana ikan kerapu memiliki habitat dengan kondisi air laut dengan kadar garam 30 - 33 ppt, kadar oksigen ± 4 ppm, temperatur air laut 240 - 310C dan kadar keasaman (pH) air laut 7,6 - 7,8. Kecepatan arus air ideal sekitar 20 hingga 40 cm/detik dimana diperlukan untuk pergantian air dan oksigen serta untuk mengalirkan sisa metabolisme ikan serta pakan ikan keluar. Kondisi habitat ikan ini harus dpat dikontrol dengan baik. Di beberapa tempat budidaya ikan kerapu sistem penjagaan kondisi habitat ini dilakukan secara manual. Dengan adanya sistem kontrol, kondisi habitat ini akan sangat mudah dijaga. Dimana dalam penelitian ini difokuskan pada kemampuan sistem kontrol kekeruhan dan temperatur air laut meliputi fungsi sensor, waktu kerja pengontrol dan kinerja peralatan kontrol. Perangkat pengontrol menggunakan microcontroller Arduino Mega dengan beberapa sensor temperatur dan kekeruhan. Sensor temperatur menggunakan tipe DS18S20 dan untuk kontrol kekeruhan menggunakan sensor turbidity. Dari hasil pengujian didapatkan bahwa sistem kontrol ini dapat mengatur dan menjaga kadar kekeruhan dan temperatur air laut dengan arus 0.215 A untuk satu relay dan 0.33 A untuk 3 relay. Untuk kekeruhan dibutuhkan waktu yang dibutuhkan untuk kontrol aktif yaitu 15 detik dengan indikator kekeruhan dari pakan ikan sebanyak 50 gram dan 10 liter air. Untuk kapasitas yang lain 15 liter air didapatkan waktu kontrol aktif pada 40 detik dengan jumlah pakan 50 gram. Hal ini menunjukkan kontrol kekeruhan bekerja dengan baik dengan semakin keruh air laut semakin cepat bekerja sistem kontrol menggantikan air laut untuk tetap menjaga habitatnya. Waktu yang dibutuhkan untuk menurukan temperatur 1.270C adalah 6 menit 37 detik dengan kapasitas 10 lite

Systematic Comparison of Reverse Phase and Hydrophilic Interaction Liquid Chromatography Platforms for the Analysis of N‑Linked Glycans

Due to the hydrophilic nature of glycans, reverse phase chromatography has not been widely used as a glycomic separation technique coupled to mass spectrometry. Other approaches such as hydrophilic interaction chromatography and porous graphitized carbon chromatography are often employed, though these strategies frequently suffer from decreased chromatographic resolution, long equilibration times, indefinite retention, and column bleed. Herein, it is shown that, through an efficient hydrazone formation derivatization of N-linked glycans (∼4 h of additional sample preparation time which is carried out in parallel), numerous experimental and practical advantages are gained when analyzing the glycans by online reverse phase chromatography. These benefits include an increased number of glycans detected, increased peak capacity of the separation, and the ability to analyze glycans on the identical liquid chromatography–mass spectrometry platform commonly used for proteomic analyses. The data presented show that separation of derivatized N-linked glycans by reverse phase chromatography significantly out-performs traditional separation of native or derivatized glycans by hydrophilic interaction chromatography. Furthermore, the movement to a more ubiquitous separation technique will afford numerous research groups the opportunity to analyze both proteomic and glycomic samples on the same platform with minimal time and physical change between experiments, increasing the efficiency of “multiomic” biological approaches

Global Proteomic Analysis of Functional Compartments in Immature Avian Follicles Using Laser Microdissection Coupled to LC-MS/MS

Laser microdissection (LMD) was utilized for the separation of the yolk, follicular wall (granulosa and theca), and surrounding stromal cells of small white follicles (SWF) obtained from reproductively active domestic fowl. Herein, we provide an in situ proteomics-based approach to studying follicular development through the use of LMD and mass spectrometry. This study resulted in a total of 2889 proteins identified from the three specific isolated compartments. White yolk from the smallest avian follicles resulted in the identification of 1984 proteins, while isolated follicular wall and ovarian stroma yielded 2470 and 2456 proteins, respectively. GO annotations highlighted the functional differences between the compartments. Among the three compartments examined, the relative abundance of vitellogenins, steroidogenic enzymes, anti-Mullerian hormone, transcription factors, and proteins involved in retinoic acid receptors/retinoic acid synthesis, transcription factors, and cell surface receptors such as EGFR and their associated signaling pathways reflected known cellular function of the ovary. This study has provided a global proteome for SWF, white yolk, and ovarian stroma of the avian ovary that can be used as a baseline for future studies and verifies that the coupling of LMD with proteomic analysis can be used to evaluate proteins from small, physiologically functional compartments of complex tissue

Direct Analysis of Textile Fabrics and Dyes Using Infrared Matrix-Assisted Laser Desorption Electrospray Ionization Mass Spectrometry

The forensic analysis of textile fibers uses a variety of techniques from microscopy to spectroscopy. One such technique that is often used to identify the dye(s) within the fiber is mass spectrometry (MS). In the traditional MS method, the dye must be extracted from the fabric and the dye components are separated by chromatography prior to mass spectrometric analysis. Direct analysis of the dye from the fabric allows the omission of the lengthy sample preparation involved in extraction, thereby significantly reducing the overall analysis time. Herein, a direct analysis of dyed textile fabric was performed using the infrared matrix-assisted laser desorption electrospray ionization (IR-MALDESI) source for MS. In MALDESI, an IR laser with wavelength tuned to 2.94 μm is used to desorb the dye from the fabric sample with the aid of water as the matrix. The desorbed dye molecules are then postionized by electrospray ionization (ESI). A variety of dye classes were analyzed from various fabrics with little to no sample preparation allowing for the identification of the dye mass and in some cases the fiber polymer. Those dyes that were not detected using MALDESI were also not observed by direct infusion ESI of the dye standard

Cacalia indet.

The filamentous fungus <i>Magnaporthe oryzae</i> (<i>M. oryzae</i>) is the causative agent of rice blast disease and presents a significant threat to worldwide rice production. To establish the groundwork for future research on the pathogenic development of <i>M. oryzae</i>, a global proteomic study of conidia was performed. The filter aided sample preparation method (FASP) and anion StageTip fractionation combined with long, optimized shallow 210 min nanoLC gradients prior to mass spectrometry analysis on an Orbitrap XL was applied, which resulted in a doubling of protein identifications in comparison to our previous GeLC analysis. Herein, we report the identification of 2912 conidial proteins at a 1% protein false discovery rate (FDR) and we present the most extensive study performed on <i>M. oryzae</i> conidia to date. A similar distribution between identified proteins and the predicted proteome was observed when subcellular localization analysis was performed, suggesting the detected proteins build a representative portion of the predicted proteome. A higher percentage of cytoplasmic proteins (associated with translation, energy, and metabolism) were observed in the conidial proteome relative to the whole predicted proteome. Conversely, nuclear and extracellular proteins were less well represented in the conidial proteome. Further analysis by gene ontology revealed biological insights into identified proteins important for central metabolic processes and the physiology of conidia

The PeptideAtlas of the Domestic Laying Hen

Proteomics-based biological research is greatly expanded by high-quality mass spectrometry studies, which are themselves enabled by access to quality mass spectrometry resources, such as high-quality curated proteome data repositories. We present a PeptideAtlas for the domestic chicken, containing an extensive and robust collection of chicken tissue and plasma samples with substantial value for the chicken proteomics community for protein validation and design of downstream targeted proteome quantitation. The chicken PeptideAtlas contains 6646 canonical proteins at a protein FDR of 1.3%, derived from ∼100 000 peptides at a peptide level FDR of 0.1%. The rich collection of readily accessible data is easily mined for the purposes of data validation and experimental planning, particularly in the realm of developing proteome quantitation workflows. Herein we demonstrate the use of the atlas to mine information on common chicken acute-phase proteins and biomarkers for cancer detection research, as well as their localization and polymorphisms. This wealth of information will support future proteome-based research using this highly important agricultural organism in pursuit of both chicken and human health outcomes

VtgC affinity purification coupled to tandem mass spectrometry.

<p>VtgC affinity purification coupled to tandem mass spectrometry.</p

Confocal microscopy of anti-VtgC coupled to DyLight633.

<p>Confocal microscopy images of immunohistochemistry of mature female white perch ovary tissues across one reproductive year stained with anti-VtgC coupled to DyLight633: (A) pre-vitellogenic (PreVG), (B) early-vitellogenic (EVG), (C) mid-vitellogenic (MVG), and (D) post-vitellogenic (PostVG) ovary sections.</p

In-Depth Analysis of the <i>Magnaporthe oryzae</i> Conidial Proteome

The filamentous fungus <i>Magnaporthe oryzae</i> (<i>M. oryzae</i>) is the causative agent of rice blast disease and presents a significant threat to worldwide rice production. To establish the groundwork for future research on the pathogenic development of <i>M. oryzae</i>, a global proteomic study of conidia was performed. The filter aided sample preparation method (FASP) and anion StageTip fractionation combined with long, optimized shallow 210 min nanoLC gradients prior to mass spectrometry analysis on an Orbitrap XL was applied, which resulted in a doubling of protein identifications in comparison to our previous GeLC analysis. Herein, we report the identification of 2912 conidial proteins at a 1% protein false discovery rate (FDR) and we present the most extensive study performed on <i>M. oryzae</i> conidia to date. A similar distribution between identified proteins and the predicted proteome was observed when subcellular localization analysis was performed, suggesting the detected proteins build a representative portion of the predicted proteome. A higher percentage of cytoplasmic proteins (associated with translation, energy, and metabolism) were observed in the conidial proteome relative to the whole predicted proteome. Conversely, nuclear and extracellular proteins were less well represented in the conidial proteome. Further analysis by gene ontology revealed biological insights into identified proteins important for central metabolic processes and the physiology of conidia

White perch LR8 and Lrp13 western blotting.

<p>Results of western blotting for the two white perch vitellogenin receptors in female liver, plasma, and ovary tissues sampled across one reproductive year during pre-vitellogenesis (PreVG), early-vitellogenesis (EVG), mid-vitellogenesis (MVG), and post-vitellogenesis (PostVG) across three biological replicates.</p