2019
DOI: 10.3390/md17070397
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Quantitative Proteome Reveals Variation in the Condition Factor of Sea Urchin Strongylocentrotus nudus during the Fishing Season Using an iTRAQ-based Approach

Abstract: To investigate the variation in the condition factor of the sea urchin Strongylocentrotus nudus (S. nudus), gonads were collected in May (MAY), June (JUN), and July (JUL), at the beginning (AUG-b) and end of August (AUG-e). Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) detection of the gonads revealed an obvious enhancement of the band at about 37 kDa from July, which was identified as transforming growth factor-beta-induced protein ig-h3 (TGFBI) by nanoLC-ESI-MS/MS. Gonadal proteins wer… Show more

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Cited by 2 publications
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“…In the gill of tropical marbled eel, salinity acclimation proteins were analyzed by iTRAQ proteomic method [ 26 ]. The significant correlation between gonadal index (GI) and protein content might play key roles in changing the condition factor of gonads in sea urchin Strongylocentrotus nudus [ 27 ]. The proteome of carp sperm between the immobilized and activated spermatozoa mainly involved in ubiquitin‒proteasome pathways, glycolysis, the TCA cycle, and remodeling related to sperm energy metabolism and motility [ 28 ].…”
Section: Discussionmentioning
confidence: 99%
“…In the gill of tropical marbled eel, salinity acclimation proteins were analyzed by iTRAQ proteomic method [ 26 ]. The significant correlation between gonadal index (GI) and protein content might play key roles in changing the condition factor of gonads in sea urchin Strongylocentrotus nudus [ 27 ]. The proteome of carp sperm between the immobilized and activated spermatozoa mainly involved in ubiquitin‒proteasome pathways, glycolysis, the TCA cycle, and remodeling related to sperm energy metabolism and motility [ 28 ].…”
Section: Discussionmentioning
confidence: 99%
“…The protein profile of the extracted proteins was obtained by SDS-PAGE, according to the protocol described by Shang et al (2019) with some modifications. Briefly, 20 µg of each protein sample in loading buffer was heated at 95°C for 5 min and then centrifuged at 25,000 × g for 5 min.…”
Section: Methodsmentioning
confidence: 99%