Enhancement of insect antifreeze protein activity by solutes of low molecular mass.
Identifieur interne : 003A05 ( Main/Exploration ); précédent : 003A04; suivant : 003A06Enhancement of insect antifreeze protein activity by solutes of low molecular mass.
Auteurs : N. Li [États-Unis] ; C A Andorfer ; J G DumanSource :
- The Journal of experimental biology [ 0022-0949 ] ; 1998.
Descripteurs français
- KwdFr :
- ADN complémentaire (génétique), ADN complémentaire (isolement et purification), ARN (isolement et purification), Acclimatation (physiologie), Acide citrique (pharmacologie), Animaux, Chromatographie en phase liquide à haute performance, Congélation, Données de séquences moléculaires, Glace, Glycoprotéines (génétique), Glycoprotéines (isolement et purification), Glycoprotéines (métabolisme), Larve, Masse moléculaire, Protéines antigel, Protéines d'insecte (génétique), Protéines d'insecte (isolement et purification), Protéines d'insecte (métabolisme), Solutions, Séquence d'acides aminés, Séquence nucléotidique, Techniques in vitro.
- MESH :
- génétique : ADN complémentaire, Glycoprotéines, Protéines d'insecte.
- isolement et purification : ADN complémentaire, ARN, Glycoprotéines, Protéines d'insecte.
- métabolisme : Glycoprotéines, Protéines d'insecte.
- pharmacologie : Acide citrique.
- physiologie : Acclimatation.
- Animaux, Chromatographie en phase liquide à haute performance, Congélation, Données de séquences moléculaires, Glace, Larve, Masse moléculaire, Protéines antigel, Solutions, Séquence d'acides aminés, Séquence nucléotidique, Techniques in vitro.
English descriptors
- KwdEn :
- Acclimatization (physiology), Amino Acid Sequence, Animals, Antifreeze Proteins, Base Sequence, Chromatography, High Pressure Liquid, Citric Acid (pharmacology), Coleoptera (metabolism), DNA, Complementary (genetics), DNA, Complementary (isolation & purification), Freezing, Glycoproteins (genetics), Glycoproteins (isolation & purification), Glycoproteins (metabolism), Ice, In Vitro Techniques, Insect Proteins (genetics), Insect Proteins (isolation & purification), Insect Proteins (metabolism), Larva, Molecular Sequence Data, Molecular Weight, RNA (isolation & purification), Solutions.
- MESH :
- chemical , genetics : DNA, Complementary, Glycoproteins, Insect Proteins.
- chemical , isolation & purification : DNA, Complementary, Glycoproteins, Insect Proteins, RNA.
- chemical , metabolism : Glycoproteins, Insect Proteins.
- chemical , pharmacology : Citric Acid.
- chemical : Antifreeze Proteins, Ice, Solutions.
- metabolism : Coleoptera.
- physiology : Acclimatization.
- Amino Acid Sequence, Animals, Base Sequence, Chromatography, High Pressure Liquid, Freezing, In Vitro Techniques, Larva, Molecular Sequence Data, Molecular Weight.
Abstract
Antifreeze proteins (AFPs) lower the non-equilibrium freezing point of water (in the presence of ice) below the melting point, thereby producing a difference between the freezing and melting points that has been termed thermal hysteresis. In general, the magnitude of the thermal hysteresis depends upon the specific activity and concentration of the AFP. This study describes several low-molecular-mass solutes that enhance the thermal hysteresis activity of an AFP from overwintering larvae of the beetle Dendroides canadensis. The most active of these is citrate, which increases the thermal hysteresis nearly sixfold from 1.2 degrees C in its absence to 6.8 degrees C. Solutes which increase activity approximately fourfold are succinate, malate, aspartate, glutamate and ammonium sulfate. Glycerol, sorbitol, alanine and ammonium bicarbonate increased thermal hysteresis approximately threefold. Interestingly, 0.5 mol l-1 sodium sulfate eliminated activity. Solute concentrations between 0.25 and 1 mol l-1 were generally required to elicit optimal thermal hysteresis activity. Glycerol is the only one of these enhancing solutes that is known to be present at these concentrations in overwintering D. canadensis, and therefore the physiological significance of most of these enhancers is unknown. The mechanism(s) of this enhancement is also unknown. The AFP used in this study (DAFP-4) is nearly identical to previously described D. canadensis AFPs. The mature protein consists of 71 amino acid residues arranged in six 12- or 13-mer repeats with a consensus sequence consisting of Cys-Thr-X3-Ser-X5-X6-Cys-X8-X9-Ala-X11-Thr-X1 3, where X3 and X11 tend to be charged residues, X5 tends to be Thr or Ser, X6 to be Asn or Asp, X9 to be Asn or Lys and X13 to be Ala in the 13-mers. DAFP-4 is shorter by one repeat than previously described D. canadensis AFPs.
PubMed: 9662495
Affiliations:
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Le document en format XML
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Li</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biological Sciences, University of Notre Dame, Notre Dame, IN 46556, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, University of Notre Dame, Notre Dame, IN 46556</wicri:regionArea><placeName><region type="state">Indiana</region></placeName></affiliation></author><author><name sortKey="Andorfer, C A" sort="Andorfer, C A" uniqKey="Andorfer C" first="C A" last="Andorfer">C A Andorfer</name></author><author><name sortKey="Duman, J G" sort="Duman, J G" uniqKey="Duman J" first="J G" last="Duman">J G Duman</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1998">1998</date><idno type="RBID">pubmed:9662495</idno><idno type="pmid">9662495</idno><idno type="wicri:Area/PubMed/Corpus">002680</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002680</idno><idno type="wicri:Area/PubMed/Curation">002680</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002680</idno><idno type="wicri:Area/PubMed/Checkpoint">002538</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002538</idno><idno type="wicri:Area/Ncbi/Merge">002B24</idno><idno type="wicri:Area/Ncbi/Curation">002B24</idno><idno type="wicri:Area/Ncbi/Checkpoint">002B24</idno><idno type="wicri:doubleKey">0022-0949:1998:Li N:enhancement:of:insect</idno><idno type="wicri:Area/Main/Merge">003A53</idno><idno type="wicri:Area/Main/Curation">003A05</idno><idno type="wicri:Area/Main/Exploration">003A05</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Enhancement of insect antifreeze protein activity by solutes of low molecular mass.</title><author><name sortKey="Li, N" sort="Li, N" uniqKey="Li N" first="N" last="Li">N. Li</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biological Sciences, University of Notre Dame, Notre Dame, IN 46556, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, University of Notre Dame, Notre Dame, IN 46556</wicri:regionArea><placeName><region type="state">Indiana</region></placeName></affiliation></author><author><name sortKey="Andorfer, C A" sort="Andorfer, C A" uniqKey="Andorfer C" first="C A" last="Andorfer">C A Andorfer</name></author><author><name sortKey="Duman, J G" sort="Duman, J G" uniqKey="Duman J" first="J G" last="Duman">J G Duman</name></author></analytic><series><title level="j">The Journal of experimental biology</title><idno type="ISSN">0022-0949</idno><imprint><date when="1998" type="published">1998</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acclimatization (physiology)</term><term>Amino Acid Sequence</term><term>Animals</term><term>Antifreeze Proteins</term><term>Base Sequence</term><term>Chromatography, High Pressure Liquid</term><term>Citric Acid (pharmacology)</term><term>Coleoptera (metabolism)</term><term>DNA, Complementary (genetics)</term><term>DNA, Complementary (isolation & purification)</term><term>Freezing</term><term>Glycoproteins (genetics)</term><term>Glycoproteins (isolation & purification)</term><term>Glycoproteins (metabolism)</term><term>Ice</term><term>In Vitro Techniques</term><term>Insect Proteins (genetics)</term><term>Insect Proteins (isolation & purification)</term><term>Insect Proteins (metabolism)</term><term>Larva</term><term>Molecular Sequence Data</term><term>Molecular Weight</term><term>RNA (isolation & purification)</term><term>Solutions</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (génétique)</term><term>ADN complémentaire (isolement et purification)</term><term>ARN (isolement et 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qualifier="isolation & purification" xml:lang="en"><term>DNA, Complementary</term><term>Glycoproteins</term><term>Insect Proteins</term><term>RNA</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glycoproteins</term><term>Insect Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Citric Acid</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Antifreeze Proteins</term><term>Ice</term><term>Solutions</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN complémentaire</term><term>Glycoprotéines</term><term>Protéines d'insecte</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>ADN complémentaire</term><term>ARN</term><term>Glycoprotéines</term><term>Protéines d'insecte</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coleoptera</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines</term><term>Protéines d'insecte</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acide citrique</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Acclimatation</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Acclimatization</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Chromatography, High Pressure Liquid</term><term>Freezing</term><term>In Vitro Techniques</term><term>Larva</term><term>Molecular Sequence Data</term><term>Molecular Weight</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Chromatographie en phase liquide à haute performance</term><term>Congélation</term><term>Données de séquences moléculaires</term><term>Glace</term><term>Larve</term><term>Masse moléculaire</term><term>Protéines antigel</term><term>Solutions</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Techniques in vitro</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Antifreeze proteins (AFPs) lower the non-equilibrium freezing point of water (in the presence of ice) below the melting point, thereby producing a difference between the freezing and melting points that has been termed thermal hysteresis. In general, the magnitude of the thermal hysteresis depends upon the specific activity and concentration of the AFP. This study describes several low-molecular-mass solutes that enhance the thermal hysteresis activity of an AFP from overwintering larvae of the beetle Dendroides canadensis. The most active of these is citrate, which increases the thermal hysteresis nearly sixfold from 1.2 degrees C in its absence to 6.8 degrees C. Solutes which increase activity approximately fourfold are succinate, malate, aspartate, glutamate and ammonium sulfate. Glycerol, sorbitol, alanine and ammonium bicarbonate increased thermal hysteresis approximately threefold. Interestingly, 0.5 mol l-1 sodium sulfate eliminated activity. Solute concentrations between 0.25 and 1 mol l-1 were generally required to elicit optimal thermal hysteresis activity. Glycerol is the only one of these enhancing solutes that is known to be present at these concentrations in overwintering D. canadensis, and therefore the physiological significance of most of these enhancers is unknown. The mechanism(s) of this enhancement is also unknown. The AFP used in this study (DAFP-4) is nearly identical to previously described D. canadensis AFPs. The mature protein consists of 71 amino acid residues arranged in six 12- or 13-mer repeats with a consensus sequence consisting of Cys-Thr-X3-Ser-X5-X6-Cys-X8-X9-Ala-X11-Thr-X1 3, where X3 and X11 tend to be charged residues, X5 tends to be Thr or Ser, X6 to be Asn or Asp, X9 to be Asn or Lys and X13 to be Ala in the 13-mers. DAFP-4 is shorter by one repeat than previously described D. canadensis AFPs.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Indiana</li></region></list><tree><noCountry><name sortKey="Andorfer, C A" sort="Andorfer, C A" uniqKey="Andorfer C" first="C A" last="Andorfer">C A Andorfer</name><name sortKey="Duman, J G" sort="Duman, J G" uniqKey="Duman J" first="J G" last="Duman">J G Duman</name></noCountry><country name="États-Unis"><region name="Indiana"><name sortKey="Li, N" sort="Li, N" uniqKey="Li N" first="N" last="Li">N. Li</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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