Proteome analysis of Persian sturgeon (Acipenser persicus) ova.
Identifieur interne : 000A53 ( Main/Merge ); précédent : 000A52; suivant : 000A54Proteome analysis of Persian sturgeon (Acipenser persicus) ova.
Auteurs : Saeed Keyvanshokooh [Iran] ; Behrouz VaziriSource :
- Animal reproduction science [ 1873-2232 ] ; 2008.
English descriptors
- KwdEn :
- Animals, Egg Proteins (chemistry), Egg Proteins (isolation & purification), Electrophoresis, Gel, Two-Dimensional, Energy Metabolism, Enzymes (chemistry), Enzymes (isolation & purification), Female, Fishes (genetics), Ovulation, Ovum (physiology), Peptide Mapping, Proteins (chemistry), Proteins (genetics), Proteins (isolation & purification), Proteome (genetics), Proteomics (methods), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Trypsin, Vitellogenins (chemistry), Vitellogenins (isolation & purification).
- MESH :
- chemical , chemistry : Egg Proteins, Enzymes, Proteins, Vitellogenins.
- chemical , genetics : Proteins, Proteome.
- chemical , isolation & purification : Egg Proteins, Enzymes, Proteins, Vitellogenins.
- genetics : Fishes.
- methods : Proteomics.
- physiology : Ovum.
- Animals, Electrophoresis, Gel, Two-Dimensional, Energy Metabolism, Female, Ovulation, Peptide Mapping, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Trypsin.
Abstract
The Persian sturgeon ova are a key material both for inevitable artificial propagation and for caviar production. In this study, the proteome profile of Persian sturgeon ova was analyzed using 2-DE and MALDI-TOF/TOF in order to determine its protein composition. Out of 192 spots analyzed with MALDI-TOF/TOF, 107 spots corresponding to 73 different proteins were identified. The identified proteins were classified into 11 groups with regard to their main known function involving cell structure (24.65%), translation and transcription (12.32%), metabolism and energy production (12.32%), protein synthesis (9.60%), membrane protein receptors or cell signaling (8.21%), cell defense (5.47%), transport (5.47%), cell division (8.21%), vitellogenin (2.73%), unclassified (6.84%) and unknown function (4.10%). The results of this study provide a valuable resource for molecular analysis of normal and abnormal conditions affecting female reproduction. Moreover, it may help to better understand factors affecting caviar quality during refrigerated storage.
DOI: 10.1016/j.anireprosci.2007.10.008
PubMed: 18054827
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sort="Keyvanshokooh, Saeed" uniqKey="Keyvanshokooh S" first="Saeed" last="Keyvanshokooh">Saeed Keyvanshokooh</name><affiliation wicri:level="1"><nlm:affiliation>Department of Fisheries, College of Marine Natural Resources, Khorramshahr University of Marine Science and Technology, Khorramshahr, Iran.</nlm:affiliation><country xml:lang="fr">Iran</country><wicri:regionArea>Department of Fisheries, College of Marine Natural Resources, Khorramshahr University of Marine Science and Technology, Khorramshahr</wicri:regionArea><wicri:noRegion>Khorramshahr</wicri:noRegion></affiliation></author><author><name sortKey="Vaziri, Behrouz" sort="Vaziri, Behrouz" uniqKey="Vaziri B" first="Behrouz" last="Vaziri">Behrouz Vaziri</name></author></analytic><series><title level="j">Animal reproduction science</title><idno type="eISSN">1873-2232</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Egg Proteins (chemistry)</term><term>Egg Proteins (isolation & purification)</term><term>Electrophoresis, Gel, Two-Dimensional</term><term>Energy Metabolism</term><term>Enzymes (chemistry)</term><term>Enzymes (isolation & purification)</term><term>Female</term><term>Fishes (genetics)</term><term>Ovulation</term><term>Ovum (physiology)</term><term>Peptide Mapping</term><term>Proteins (chemistry)</term><term>Proteins (genetics)</term><term>Proteins (isolation & purification)</term><term>Proteome (genetics)</term><term>Proteomics (methods)</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term><term>Trypsin</term><term>Vitellogenins (chemistry)</term><term>Vitellogenins (isolation & purification)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Egg Proteins</term><term>Enzymes</term><term>Proteins</term><term>Vitellogenins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Proteins</term><term>Proteome</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Egg Proteins</term><term>Enzymes</term><term>Proteins</term><term>Vitellogenins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Fishes</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Proteomics</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Ovum</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Electrophoresis, Gel, Two-Dimensional</term><term>Energy Metabolism</term><term>Female</term><term>Ovulation</term><term>Peptide Mapping</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term><term>Trypsin</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Persian sturgeon ova are a key material both for inevitable artificial propagation and for caviar production. In this study, the proteome profile of Persian sturgeon ova was analyzed using 2-DE and MALDI-TOF/TOF in order to determine its protein composition. Out of 192 spots analyzed with MALDI-TOF/TOF, 107 spots corresponding to 73 different proteins were identified. The identified proteins were classified into 11 groups with regard to their main known function involving cell structure (24.65%), translation and transcription (12.32%), metabolism and energy production (12.32%), protein synthesis (9.60%), membrane protein receptors or cell signaling (8.21%), cell defense (5.47%), transport (5.47%), cell division (8.21%), vitellogenin (2.73%), unclassified (6.84%) and unknown function (4.10%). The results of this study provide a valuable resource for molecular analysis of normal and abnormal conditions affecting female reproduction. Moreover, it may help to better understand factors affecting caviar quality during refrigerated storage.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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