Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR6457701_1.fastq.gz | Fastqsanger.gz | |||
| SRR6457701_2.fastq.gz | Fastqsanger.gz | |||
| SRR6457702_1.fastq.gz | Fastqsanger.gz | |||
| SRR6457702_2.fastq.gz | Fastqsanger.gz | |||
| SRR6674898_1.fastq.gz | Fastqsanger.gz |
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Project description:To investigate the central control of water homeostasis in the dromedary camel, we have performed transcriptomic studies on the supraoptic nucleus samples from camels under control (water ad libitum) and dehydrated (water deprivation for 20 days) conditions by RNA sequencing. We have identified genes that change in expression in response to hyperosmotic challenge and transcriptomic response networks that might be essential for adaptations of camel to live and thrive in aird desert environment.
2022-08-23 | GSE198577 | GEO
Project description:dromedary camel milk microbiome Raw sequence reads
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Project description:Dromedary camel Mitochondrial Genome
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Project description:Camel milk is widely characterized with regard to caseins and whey proteins. However, in camelids, close to nothing is known about the Milk Fat Globule Membrane (MFGM), the membrane surrounding fat globules in milk. The purpose of this study was thus to identify MFGM proteins from Camelus dromedarius milk. Major MFGM proteins (namely, fatty acid synthase, xanthine oxidase, butyrophilin, lactadherin, and adipophilin) already evidenced in cow milk were identified in camel milk using mass spectrometry. In addition, a 1D-LC-MS/MS approach led us to identify 322 functional groups of proteins associated with the camel Milk Fat Globule Membrane. We hope that these findings will contribute to a better characterization of camel milk and to an improved understanding of lipid droplet formation in the mammary epithelial cell.
2013-02-05 | PXD000059 | Pride
Project description:Camel milk is considered one of the most valuable food sources for nomadic people in arid and semi-arid areas and has also been consumed as a natural adjuvant for managing a variety of human diseases for centuries due to its nutritional values and extraordinary medicinal properties. A total of 180 milk samples were collected from Bikaneri and Jaisalmeri camels during various seasons in the Jodhpur and Sikar districts of Rajasthan for the proteomics study. Protein profiling of camel milk was done by LC-MS/MS. The protein pellets were prepared from 50 mL of pooled raw milk. The trypsinization and clean-up protocol was performed using standard methods. Then, Mass spectrometric analysis of peptide mixtures was performed using the EASY-nLC 1200 system coupled to a Thermo Fisher-Q Exactive equipped with a nanoelectrospray ion source. All samples were processed and analyzed with Proteome Discoverer (v2.4) against the Uniprot camel reference proteome database. A total of 704 protein groups were identified in the milk of Bikaneri and Jaisalmeri camels on the Uniprot Camelus dromedarius Database. There were 21 (3%) and 17 (2.4%) unique protein groups with 666 (94.6%) common proteins in the milk of Bikaneri and Jaisalmeri, respectively. In addition, 687 (97%) and 683 (98%) specific proteins were found in Bikaneri and Jaisalmeri camel milk, respectively. The camel casein components (CNs) were found as αs1-CN, αs2-CN, β- CN and κ-CN. Whey protein such as β-lactoglobulin was not found in the camel milk but α- lactalbumin was abundant. Breed variation was less observed because only 18 significantly expressed proteins were obtained in the milk of the Bikaneri and Jaisalmeri camel breeds.
2025-09-22 | PXD058940 | Pride
Project description:In this project, spray drying and low temperature vacuum drying were used to produce camel milk powder, and the effects of two technologies on the abundance and biological function of bioactive proteins in camel milk were compared. The results showed that low temperature vacuum drying retained more active proteins, which was related to immune response-related functions and directly affected the nutritional value of camel milk powder.
2025-09-11 | PXD068282 |
Project description:Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190°C - 250°C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. This study provides useful insights for optimization of CM powder production.
2021-02-25 | PXD023290 | Pride
Project description:The one-humped Arabian camel (Camelus dromedarius) is the most important livestock animal in arid and semi-arid regions and continues to provide basic necessities to millions of people. In the current context of global warming, there is renewed interest in the adaptive mechanisms that enable camelids to survive in arid conditions. Recent investigations described genomic signatures that revealed evolutionary adaptations to desert environments. We now present a comprehensive catalogue of the transcriptomes and proteomes of the dromedary kidney and describe how the gene expression profiles of Differentially Expressed Genes (DEGs) are modulated as a consequence of chronic dehydration and subsequent acute rehydration. We performed RNAseq and quantification of peptides in samples from 15 dromedaries (5 controls, 5 dehydrated and 5 rehydrated). Gene Ontology analyses suggested an enrichment of the cholesterol biosynthetic process and an overrepresentation of categories related to “ion transmembrane transport” in the camel kidney, and RTN analyses confirmed alterations in the transcriptional machinery involved in cholesterol synthesis. These data were validated by RT-qPCR. Based on our hypothesis of a role for cholesterol during dehydration, we identified DEGs with roles in the countercurrent multiplication process which are affected by changes in the level of cholesterol. Thus, we further validated 3 genes coding for ion transporting proteins (KCNJ8, SLC9A7 and ATP1B3) and AQP2, which were upregulated during dehydration. Our datasets suggest that suppression of cholesterol biosynthesis may facilitate water retention in the kidney of the dromedary by indirectly enhancing the osmotic gradient along the medullary interstitium and the AQP2-mediated water reabsorption.
2021-06-21 | PXD025644 | Pride