Nongenetic variation, genetic-environmental interactions and altered gene expression. III. Prosttranslational modifications
Identifieur interne : 003C56 ( Main/Exploration ); précédent : 003C55; suivant : 003C57Nongenetic variation, genetic-environmental interactions and altered gene expression. III. Prosttranslational modifications
Auteurs : William J. Poly [États-Unis]Source :
- Comparative Biochemistry and Physiology, Part A: Physiology [ 0300-9629 ] ; 1997.
English descriptors
- Teeft :
- Acad, Academic press, Acetylation, Acetylcholinesterase, Ache, Acta, Alcohol dehydrogenase, Amino, Amino acid, Amino acids, Aminotransferase, Bche, Biochem, Biochemistry, Biochim, Biol, Biophys, Blood grps biochem, Boca, Boca raton, Carbamylation, Carbohydrate, Carbohydrate moiety, Catalase, Chem, Clin, Comp, Conformational, Conformational changes, Current topics, Deamidation, Dehydrogenase, Dismutase, Drosophila, Edta, Electrophoresis, Electrophoretic, Electrophoretic mobility, Elsevier science, Enzyme, Enzymol, Feb, Febs lett, G6pdh, Gene expression, Genet, Genetic, Genetic control, Genetic studies, Genetic variation, Genetics, Glycoprotein, Heparin, Heterogeneity, Human serum, Human serum cholinesterase, Isoenzymes, Isomerase, Isozyme, Isozymes, Kinase, Lactate, Lactate dehydrogenase, Liss, Locus, Lysine, Markert, Medical research, Methods enzymol, Mobility, Modification, Molecular structure, Multiple enzyme forms, Multiple forms, Muscle esterases, Natl, Nongenetic, Nongenetic variation, Partial characterization, Phenotype, Phosphatase, Phosphorylation, Physiol, Poly, Polymorphism, Posttranslational, Posttranslational changes, Posttranslational covalent modifications, Posttranslational modification, Posttranslational modifications, Prairie rattlesnake, Primary structure, Proc, Proteolytic, Proteolytic modification, Quaternary structure, Rainbow trout, Rattazzi, Rothe, Scandalios, Schauer, Secondary isozyme formation, Secondary isozymes, Sialic, Sialic acids, Single gene, Societies press, Stratil, Subunit, Sulfhydryl, Sulfhydryl groups, Superoxide, Superoxide dismutase, Tion, Transferrin, Tyrosine transaminase, Whitt, Zool.
Abstract
Abstract: The use of protein electrophoretic data for determining the relationships among species or populations is widespread and generally accepted. However, posttranslational modifications have been discovered in many of the commonly analyzed proteins and enzymes. Posttranslational modifications often alter the electrophoretic mobility of the modified enzyme or protein. Because posttranslational modifications may affect only a fraction of the total enzyme or protein, an additional staining band often appears on gels as a result, and this may confound interpretations. Deamidation, acteylation, proteolytic modification, and oxidation of sulfhydryl groups are modifications that often result in an electrophoretic mobility shift. Sialic acid-induced heterogeneity has been documented for many enzymes, but neuraminidase treatment can often remove sialic acids and produce gel patterns that are easier to interpret. In some cases, ontogenetic and tissue-specific expression may be due to posttranslational modifications rather than gene control and restricted expression, respectively. Methods of preventing, detecting and eliminating posttranslational modifications are discussed. Some posttranslational modifications may be useful for detecting cryptic genetic polymorphisms.
Url:
DOI: 10.1016/S0300-9629(96)00041-2
Affiliations:
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III. Prosttranslational modifications</title><author><name sortKey="Poly, William J" sort="Poly, William J" uniqKey="Poly W" first="William J." last="Poly">William J. Poly</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Zoology, Southern Illinois University, Carbondale, IL</wicri:regionArea><wicri:noRegion>IL</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Comparative Biochemistry and Physiology, Part A: Physiology</title><title level="j" type="abbrev">CBAOLD</title><idno type="ISSN">0300-9629</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997">1997</date><biblScope unit="volume">118</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="551">551</biblScope><biblScope unit="page" to="572">572</biblScope></imprint><idno type="ISSN">0300-9629</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0300-9629</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Academic press</term><term>Acetylation</term><term>Acetylcholinesterase</term><term>Ache</term><term>Acta</term><term>Alcohol dehydrogenase</term><term>Amino</term><term>Amino acid</term><term>Amino acids</term><term>Aminotransferase</term><term>Bche</term><term>Biochem</term><term>Biochemistry</term><term>Biochim</term><term>Biol</term><term>Biophys</term><term>Blood grps biochem</term><term>Boca</term><term>Boca raton</term><term>Carbamylation</term><term>Carbohydrate</term><term>Carbohydrate moiety</term><term>Catalase</term><term>Chem</term><term>Clin</term><term>Comp</term><term>Conformational</term><term>Conformational changes</term><term>Current topics</term><term>Deamidation</term><term>Dehydrogenase</term><term>Dismutase</term><term>Drosophila</term><term>Edta</term><term>Electrophoresis</term><term>Electrophoretic</term><term>Electrophoretic mobility</term><term>Elsevier science</term><term>Enzyme</term><term>Enzymol</term><term>Feb</term><term>Febs lett</term><term>G6pdh</term><term>Gene expression</term><term>Genet</term><term>Genetic</term><term>Genetic control</term><term>Genetic studies</term><term>Genetic variation</term><term>Genetics</term><term>Glycoprotein</term><term>Heparin</term><term>Heterogeneity</term><term>Human serum</term><term>Human serum cholinesterase</term><term>Isoenzymes</term><term>Isomerase</term><term>Isozyme</term><term>Isozymes</term><term>Kinase</term><term>Lactate</term><term>Lactate dehydrogenase</term><term>Liss</term><term>Locus</term><term>Lysine</term><term>Markert</term><term>Medical research</term><term>Methods enzymol</term><term>Mobility</term><term>Modification</term><term>Molecular structure</term><term>Multiple enzyme forms</term><term>Multiple forms</term><term>Muscle esterases</term><term>Natl</term><term>Nongenetic</term><term>Nongenetic variation</term><term>Partial characterization</term><term>Phenotype</term><term>Phosphatase</term><term>Phosphorylation</term><term>Physiol</term><term>Poly</term><term>Polymorphism</term><term>Posttranslational</term><term>Posttranslational changes</term><term>Posttranslational covalent modifications</term><term>Posttranslational modification</term><term>Posttranslational modifications</term><term>Prairie rattlesnake</term><term>Primary structure</term><term>Proc</term><term>Proteolytic</term><term>Proteolytic modification</term><term>Quaternary structure</term><term>Rainbow trout</term><term>Rattazzi</term><term>Rothe</term><term>Scandalios</term><term>Schauer</term><term>Secondary isozyme formation</term><term>Secondary isozymes</term><term>Sialic</term><term>Sialic acids</term><term>Single gene</term><term>Societies press</term><term>Stratil</term><term>Subunit</term><term>Sulfhydryl</term><term>Sulfhydryl groups</term><term>Superoxide</term><term>Superoxide dismutase</term><term>Tion</term><term>Transferrin</term><term>Tyrosine transaminase</term><term>Whitt</term><term>Zool</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The use of protein electrophoretic data for determining the relationships among species or populations is widespread and generally accepted. However, posttranslational modifications have been discovered in many of the commonly analyzed proteins and enzymes. Posttranslational modifications often alter the electrophoretic mobility of the modified enzyme or protein. Because posttranslational modifications may affect only a fraction of the total enzyme or protein, an additional staining band often appears on gels as a result, and this may confound interpretations. Deamidation, acteylation, proteolytic modification, and oxidation of sulfhydryl groups are modifications that often result in an electrophoretic mobility shift. Sialic acid-induced heterogeneity has been documented for many enzymes, but neuraminidase treatment can often remove sialic acids and produce gel patterns that are easier to interpret. In some cases, ontogenetic and tissue-specific expression may be due to posttranslational modifications rather than gene control and restricted expression, respectively. Methods of preventing, detecting and eliminating posttranslational modifications are discussed. Some posttranslational modifications may be useful for detecting cryptic genetic polymorphisms.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Poly, William J" sort="Poly, William J" uniqKey="Poly W" first="William J." last="Poly">William J. Poly</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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