EsturgeonV1, PascalFrancis, Corpus, bibRecord, 000488

Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa

Identifieur interne : 000488 ( PascalFrancis/Corpus ); précédent : 000487; suivant : 000489

Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa

Auteurs : A. Ciereszko ; K. Dabrowski ; S. I. Ochkur

Source :

Molecular reproduction and development [ 1040-452X ] ; 1996.

RBID : Pascal:96-0429133

Descripteurs français

Pascal (Inist)
- Spermatozoïde, Acrosin, Trypsin, Homologie, Activité enzymatique, Régulation, Cryoconservation, Conservation sperme, Pisces, Mâle, Acipenser fulvescens.

English descriptors

KwdEn :
- Acrosin, Cryopreservation, Enzymatic activity, Homology, Male, Pisces, Regulation(control), Sperm conservation, Spermatozoa, Trypsin.

Abstract

Acipenserid fish sperm possess trypsin-like activity, resembling acrosin activity of mammalian sperm, which can be measured by hydrolysis of N-α-benzoyl-DL-arginine p-nitroanilide (BAPNA) (Ciereszko et al., 1994 : J Exp Zool 268 :486-491). We found that this activity can be preserved when sperm is frozen on dry ice with 0.6 M sucrose-10% dimethylsulfoxide (DMSO) extender (sperm :extender ratio 1 :3), and subsequently stored in liquid nitrogen. However, other methods of freezing (without cryoprotectant at -18°C, -80°C, and -196°C) did not protect this activity. Acrosin-like activity decreased in the course of storage of milt on ice ; 88% decline was recorded after 13 days. Acrosin-like activity increased with temperature from 10°C to 30°C, but was inactivated at 40°C to about 40% as compared to the optimum temperature. Triton X-100 inhibited activity by 15% and 72% at 0.01% and 0.1% concentrations, respectively. Activity was not affected by Mg²⁺ but was inhibited by Zn²⁺ (30% and 75% in the presence of 0.1 mM and 1 mM, respectively). Maximum velocity of substrate hydrolysis was observed at 2 mM of BAPNA. Acrosin-like activity was effectively inhibited by 4'-acetamidophenyl 4-guanidinobenzoate (AGB), an inhibitor of mammalian acrosin. Sperm acrosin-like activity correlated negatively with anti-proteinase activity of seminal plasma. We conclude that sturgeon acrosin-like activity shares many properties with mammalian acrosin. On the other hand, it has some unique properties which may represent adaptations of this enzyme to the environment of external fertilization.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

A01	`01`	`1`		`@0 1040-452X`
A03		`1`		`@0 Mol. reprod. dev.`
A05				`@2 45`
A06				`@2 1`
A08	`01`	`1`	`ENG`	`@1 Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa`
A11	`01`	`1`		`@1 CIERESZKO (A.)`
A11	`02`	`1`		`@1 DABROWSKI (K.)`
A11	`03`	`1`		`@1 OCHKUR (S. I.)`
A14	`01`			`@1 School of Natural Resources, Ohio State University @2 Columbus, Ohio @3 USA @Z 1 aut. @Z 2 aut.`
A14	`02`			`@1 Center of Agrotechnology and Veterinary Sciences, Polish Academy of Sciences @2 Olsztyn @3 POL @Z 1 aut.`
A14	`03`			`@1 Institut for Problems of Cryobiology and Cryomedicine, Ukrainian Academy of Sciences @2 Kharkov @3 UKR @Z 3 aut.`
A20				`@1 72-77`
A21				`@1 1996`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 18057 @5 354000065788360100`
A44				`@0 0000 @1 © 1996 INIST-CNRS. All rights reserved.`
A45				`@0 34 ref.`
A47	`01`	`1`		`@0 96-0429133`
A60				`@1 P`
A61				`@0 A`
A64	`01`	`1`		`@0 Molecular reproduction and development`
A66	`01`			`@0 USA`
C01	`01`		`ENG`	@0 Acipenserid fish sperm possess trypsin-like activity, resembling acrosin activity of mammalian sperm, which can be measured by hydrolysis of N-α-benzoyl-DL-arginine p-nitroanilide (BAPNA) (Ciereszko et al., 1994 : J Exp Zool 268 :486-491). We found that this activity can be preserved when sperm is frozen on dry ice with 0.6 M sucrose-10% dimethylsulfoxide (DMSO) extender (sperm :extender ratio 1 :3), and subsequently stored in liquid nitrogen. However, other methods of freezing (without cryoprotectant at -18°C, -80°C, and -196°C) did not protect this activity. Acrosin-like activity decreased in the course of storage of milt on ice ; 88% decline was recorded after 13 days. Acrosin-like activity increased with temperature from 10°C to 30°C, but was inactivated at 40°C to about 40% as compared to the optimum temperature. Triton X-100 inhibited activity by 15% and 72% at 0.01% and 0.1% concentrations, respectively. Activity was not affected by Mg²⁺ but was inhibited by Zn²⁺ (30% and 75% in the presence of 0.1 mM and 1 mM, respectively). Maximum velocity of substrate hydrolysis was observed at 2 mM of BAPNA. Acrosin-like activity was effectively inhibited by 4'-acetamidophenyl 4-guanidinobenzoate (AGB), an inhibitor of mammalian acrosin. Sperm acrosin-like activity correlated negatively with anti-proteinase activity of seminal plasma. We conclude that sturgeon acrosin-like activity shares many properties with mammalian acrosin. On the other hand, it has some unique properties which may represent adaptations of this enzyme to the environment of external fertilization.
C02	`01`	`X`		`@0 002A29A`
C03	`01`	`X`	`FRE`	`@0 Spermatozoïde @5 01`
C03	`01`	`X`	`ENG`	`@0 Spermatozoa @5 01`
C03	`01`	`X`	`SPA`	`@0 Espermatozoide @5 01`
C03	`02`	`X`	`FRE`	`@0 Acrosin @2 FE @5 02`
C03	`02`	`X`	`ENG`	`@0 Acrosin @2 FE @5 02`
C03	`02`	`X`	`SPA`	`@0 Acrosin @2 FE @5 02`
C03	`03`	`X`	`FRE`	`@0 Trypsin @2 FE @5 03`
C03	`03`	`X`	`ENG`	`@0 Trypsin @2 FE @5 03`
C03	`03`	`X`	`SPA`	`@0 Trypsin @2 FE @5 03`
C03	`04`	`X`	`FRE`	`@0 Homologie @5 04`
C03	`04`	`X`	`ENG`	`@0 Homology @5 04`
C03	`04`	`X`	`SPA`	`@0 Homología @5 04`
C03	`05`	`X`	`FRE`	`@0 Activité enzymatique @5 05`
C03	`05`	`X`	`ENG`	`@0 Enzymatic activity @5 05`
C03	`05`	`X`	`SPA`	`@0 Actividad enzimática @5 05`
C03	`06`	`X`	`FRE`	`@0 Régulation @5 07`
C03	`06`	`X`	`ENG`	`@0 Regulation(control) @5 07`
C03	`06`	`X`	`GER`	`@0 Regelung @5 07`
C03	`06`	`X`	`SPA`	`@0 Regulación @5 07`
C03	`07`	`X`	`FRE`	`@0 Cryoconservation @5 08`
C03	`07`	`X`	`ENG`	`@0 Cryopreservation @5 08`
C03	`07`	`X`	`SPA`	`@0 Crioconservación @5 08`
C03	`08`	`X`	`FRE`	`@0 Conservation sperme @5 17`
C03	`08`	`X`	`ENG`	`@0 Sperm conservation @5 17`
C03	`08`	`X`	`SPA`	`@0 Conservación esperma @5 17`
C03	`09`	`X`	`FRE`	`@0 Pisces @2 NS @5 54`
C03	`09`	`X`	`ENG`	`@0 Pisces @2 NS @5 54`
C03	`09`	`X`	`SPA`	`@0 Pisces @2 NS @5 54`
C03	`10`	`X`	`FRE`	`@0 Mâle @5 55`
C03	`10`	`X`	`ENG`	`@0 Male @5 55`
C03	`10`	`X`	`SPA`	`@0 Macho @5 55`
C03	`11`	`X`	`FRE`	`@0 Acipenser fulvescens @2 NS @4 INC @5 81`
C07	`01`	`X`	`FRE`	`@0 Serine endopeptidases @2 FE`
C07	`01`	`X`	`ENG`	`@0 Serine endopeptidases @2 FE`
C07	`01`	`X`	`SPA`	`@0 Serine endopeptidases @2 FE`
C07	`02`	`X`	`FRE`	`@0 Proteinases @2 FE`
C07	`02`	`X`	`ENG`	`@0 Proteinases @2 FE`
C07	`02`	`X`	`SPA`	`@0 Proteinases @2 FE`
C07	`03`	`X`	`FRE`	`@0 Hydrolases @2 FE`
C07	`03`	`X`	`ENG`	`@0 Hydrolases @2 FE`
C07	`03`	`X`	`SPA`	`@0 Hydrolases @2 FE`
C07	`04`	`X`	`FRE`	`@0 Enzyme`
C07	`04`	`X`	`ENG`	`@0 Enzyme`
C07	`04`	`X`	`SPA`	`@0 Enzima`
C07	`05`	`X`	`FRE`	`@0 Cellule germinale @5 20`
C07	`05`	`X`	`ENG`	`@0 Germinal cell @5 20`
C07	`05`	`X`	`SPA`	`@0 Célula germinal @5 20`
C07	`06`	`X`	`FRE`	`@0 Température @5 21`
C07	`06`	`X`	`ENG`	`@0 Temperature @5 21`
C07	`06`	`X`	`GER`	`@0 Temperatur @5 21`
C07	`06`	`X`	`SPA`	`@0 Temperatura @5 21`
C07	`07`	`X`	`FRE`	`@0 Facteur milieu @5 22`
C07	`07`	`X`	`ENG`	`@0 Environmental factor @5 22`
C07	`07`	`X`	`SPA`	`@0 Factor medio @5 22`
C07	`08`	`X`	`FRE`	`@0 Vertebrata @2 NS`
C07	`08`	`X`	`ENG`	`@0 Vertebrata @2 NS`
C07	`08`	`X`	`SPA`	`@0 Vertebrata @2 NS`
N21				`@1 295`

Format Inist (serveur)

NO :	PASCAL 96-0429133 INIST
ET :	Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa
AU :	CIERESZKO (A.); DABROWSKI (K.); OCHKUR (S. I.)
AF :	School of Natural Resources, Ohio State University/Columbus, Ohio/Etats-Unis (1 aut., 2 aut.); Center of Agrotechnology and Veterinary Sciences, Polish Academy of Sciences/Olsztyn/Pologne (1 aut.); Institut for Problems of Cryobiology and Cryomedicine, Ukrainian Academy of Sciences/Kharkov/Ukraine (3 aut.)
DT :	Publication en série; Niveau analytique
SO :	Molecular reproduction and development; ISSN 1040-452X; Etats-Unis; Da. 1996; Vol. 45; No. 1; Pp. 72-77; Bibl. 34 ref.
LA :	Anglais
EA :	Acipenserid fish sperm possess trypsin-like activity, resembling acrosin activity of mammalian sperm, which can be measured by hydrolysis of N-α-benzoyl-DL-arginine p-nitroanilide (BAPNA) (Ciereszko et al., 1994 : J Exp Zool 268 :486-491). We found that this activity can be preserved when sperm is frozen on dry ice with 0.6 M sucrose-10% dimethylsulfoxide (DMSO) extender (sperm :extender ratio 1 :3), and subsequently stored in liquid nitrogen. However, other methods of freezing (without cryoprotectant at -18°C, -80°C, and -196°C) did not protect this activity. Acrosin-like activity decreased in the course of storage of milt on ice ; 88% decline was recorded after 13 days. Acrosin-like activity increased with temperature from 10°C to 30°C, but was inactivated at 40°C to about 40% as compared to the optimum temperature. Triton X-100 inhibited activity by 15% and 72% at 0.01% and 0.1% concentrations, respectively. Activity was not affected by Mg²⁺ but was inhibited by Zn²⁺ (30% and 75% in the presence of 0.1 mM and 1 mM, respectively). Maximum velocity of substrate hydrolysis was observed at 2 mM of BAPNA. Acrosin-like activity was effectively inhibited by 4'-acetamidophenyl 4-guanidinobenzoate (AGB), an inhibitor of mammalian acrosin. Sperm acrosin-like activity correlated negatively with anti-proteinase activity of seminal plasma. We conclude that sturgeon acrosin-like activity shares many properties with mammalian acrosin. On the other hand, it has some unique properties which may represent adaptations of this enzyme to the environment of external fertilization.
CC :	002A29A
FD :	Spermatozoïde; Acrosin; Trypsin; Homologie; Activité enzymatique; Régulation; Cryoconservation; Conservation sperme; Pisces; Mâle; Acipenser fulvescens
FG :	Serine endopeptidases; Proteinases; Hydrolases; Enzyme; Cellule germinale; Température; Facteur milieu; Vertebrata
ED :	Spermatozoa; Acrosin; Trypsin; Homology; Enzymatic activity; Regulation(control); Cryopreservation; Sperm conservation; Pisces; Male
EG :	Serine endopeptidases; Proteinases; Hydrolases; Enzyme; Germinal cell; Temperature; Environmental factor; Vertebrata
GD :	Regelung
SD :	Espermatozoide; Acrosin; Trypsin; Homología; Actividad enzimática; Regulación; Crioconservación; Conservación esperma; Pisces; Macho
LO :	INIST-18057.354000065788360100
ID :	96-0429133

Links to Exploration step

Pascal:96-0429133

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en" level="a">Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa</title>
<author><name sortKey="Ciereszko, A" sort="Ciereszko, A" uniqKey="Ciereszko A" first="A." last="Ciereszko">A. Ciereszko</name>
<affiliation><inist:fA14 i1="01"><s1>School of Natural Resources, Ohio State University</s1>
<s2>Columbus, Ohio</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
</inist:fA14>
</affiliation>
<affiliation><inist:fA14 i1="02"><s1>Center of Agrotechnology and Veterinary Sciences, Polish Academy of Sciences</s1>
<s2>Olsztyn</s2>
<s3>POL</s3>
<sZ>1 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Dabrowski, K" sort="Dabrowski, K" uniqKey="Dabrowski K" first="K." last="Dabrowski">K. Dabrowski</name>
<affiliation><inist:fA14 i1="01"><s1>School of Natural Resources, Ohio State University</s1>
<s2>Columbus, Ohio</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Ochkur, S I" sort="Ochkur, S I" uniqKey="Ochkur S" first="S. I." last="Ochkur">S. I. Ochkur</name>
<affiliation><inist:fA14 i1="03"><s1>Institut for Problems of Cryobiology and Cryomedicine, Ukrainian Academy of Sciences</s1>
<s2>Kharkov</s2>
<s3>UKR</s3>
<sZ>3 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">INIST</idno>
<idno type="inist">96-0429133</idno>
<date when="1996">1996</date>
<idno type="stanalyst">PASCAL 96-0429133 INIST</idno>
<idno type="RBID">Pascal:96-0429133</idno>
<idno type="wicri:Area/PascalFrancis/Corpus">000488</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa</title>
<author><name sortKey="Ciereszko, A" sort="Ciereszko, A" uniqKey="Ciereszko A" first="A." last="Ciereszko">A. Ciereszko</name>
<affiliation><inist:fA14 i1="01"><s1>School of Natural Resources, Ohio State University</s1>
<s2>Columbus, Ohio</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
</inist:fA14>
</affiliation>
<affiliation><inist:fA14 i1="02"><s1>Center of Agrotechnology and Veterinary Sciences, Polish Academy of Sciences</s1>
<s2>Olsztyn</s2>
<s3>POL</s3>
<sZ>1 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Dabrowski, K" sort="Dabrowski, K" uniqKey="Dabrowski K" first="K." last="Dabrowski">K. Dabrowski</name>
<affiliation><inist:fA14 i1="01"><s1>School of Natural Resources, Ohio State University</s1>
<s2>Columbus, Ohio</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Ochkur, S I" sort="Ochkur, S I" uniqKey="Ochkur S" first="S. I." last="Ochkur">S. I. Ochkur</name>
<affiliation><inist:fA14 i1="03"><s1>Institut for Problems of Cryobiology and Cryomedicine, Ukrainian Academy of Sciences</s1>
<s2>Kharkov</s2>
<s3>UKR</s3>
<sZ>3 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
</analytic>
<series><title level="j" type="main">Molecular reproduction and development</title>
<title level="j" type="abbreviated">Mol. reprod. dev.</title>
<idno type="ISSN">1040-452X</idno>
<imprint><date when="1996">1996</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><title level="j" type="main">Molecular reproduction and development</title>
<title level="j" type="abbreviated">Mol. reprod. dev.</title>
<idno type="ISSN">1040-452X</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acrosin</term>
<term>Cryopreservation</term>
<term>Enzymatic activity</term>
<term>Homology</term>
<term>Male</term>
<term>Pisces</term>
<term>Regulation(control)</term>
<term>Sperm conservation</term>
<term>Spermatozoa</term>
<term>Trypsin</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Spermatozoïde</term>
<term>Acrosin</term>
<term>Trypsin</term>
<term>Homologie</term>
<term>Activité enzymatique</term>
<term>Régulation</term>
<term>Cryoconservation</term>
<term>Conservation sperme</term>
<term>Pisces</term>
<term>Mâle</term>
<term>Acipenser fulvescens</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Acipenserid fish sperm possess trypsin-like activity, resembling acrosin activity of mammalian sperm, which can be measured by hydrolysis of N-α-benzoyl-DL-arginine p-nitroanilide (BAPNA) (Ciereszko et al., 1994 : J Exp Zool 268 :486-491). We found that this activity can be preserved when sperm is frozen on dry ice with 0.6 M sucrose-10% dimethylsulfoxide (DMSO) extender (sperm :extender ratio 1 :3), and subsequently stored in liquid nitrogen. However, other methods of freezing (without cryoprotectant at -18°C, -80°C, and -196°C) did not protect this activity. Acrosin-like activity decreased in the course of storage of milt on ice ; 88% decline was recorded after 13 days. Acrosin-like activity increased with temperature from 10°C to 30°C, but was inactivated at 40°C to about 40% as compared to the optimum temperature. Triton X-100 inhibited activity by 15% and 72% at 0.01% and 0.1% concentrations, respectively. Activity was not affected by Mg<sup>2+</sup>
 but was inhibited by Zn<sup>2+</sup>
 (30% and 75% in the presence of 0.1 mM and 1 mM, respectively). Maximum velocity of substrate hydrolysis was observed at 2 mM of BAPNA. Acrosin-like activity was effectively inhibited by 4'-acetamidophenyl 4-guanidinobenzoate (AGB), an inhibitor of mammalian acrosin. Sperm acrosin-like activity correlated negatively with anti-proteinase activity of seminal plasma. We conclude that sturgeon acrosin-like activity shares many properties with mammalian acrosin. On the other hand, it has some unique properties which may represent adaptations of this enzyme to the environment of external fertilization.</div>
</front>
</TEI>
<inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>1040-452X</s0>
</fA01>
<fA03 i2="1"><s0>Mol. reprod. dev.</s0>
</fA03>
<fA05><s2>45</s2>
</fA05>
<fA06><s2>1</s2>
</fA06>
<fA08 i1="01" i2="1" l="ENG"><s1>Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa</s1>
</fA08>
<fA11 i1="01" i2="1"><s1>CIERESZKO (A.)</s1>
</fA11>
<fA11 i1="02" i2="1"><s1>DABROWSKI (K.)</s1>
</fA11>
<fA11 i1="03" i2="1"><s1>OCHKUR (S. I.)</s1>
</fA11>
<fA14 i1="01"><s1>School of Natural Resources, Ohio State University</s1>
<s2>Columbus, Ohio</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
</fA14>
<fA14 i1="02"><s1>Center of Agrotechnology and Veterinary Sciences, Polish Academy of Sciences</s1>
<s2>Olsztyn</s2>
<s3>POL</s3>
<sZ>1 aut.</sZ>
</fA14>
<fA14 i1="03"><s1>Institut for Problems of Cryobiology and Cryomedicine, Ukrainian Academy of Sciences</s1>
<s2>Kharkov</s2>
<s3>UKR</s3>
<sZ>3 aut.</sZ>
</fA14>
<fA20><s1>72-77</s1>
</fA20>
<fA21><s1>1996</s1>
</fA21>
<fA23 i1="01"><s0>ENG</s0>
</fA23>
<fA43 i1="01"><s1>INIST</s1>
<s2>18057</s2>
<s5>354000065788360100</s5>
</fA43>
<fA44><s0>0000</s0>
<s1>© 1996 INIST-CNRS. All rights reserved.</s1>
</fA44>
<fA45><s0>34 ref.</s0>
</fA45>
<fA47 i1="01" i2="1"><s0>96-0429133</s0>
</fA47>
<fA60><s1>P</s1>
</fA60>
<fA61><s0>A</s0>
</fA61>
<fA64 i1="01" i2="1"><s0>Molecular reproduction and development</s0>
</fA64>
<fA66 i1="01"><s0>USA</s0>
</fA66>
<fC01 i1="01" l="ENG"><s0>Acipenserid fish sperm possess trypsin-like activity, resembling acrosin activity of mammalian sperm, which can be measured by hydrolysis of N-α-benzoyl-DL-arginine p-nitroanilide (BAPNA) (Ciereszko et al., 1994 : J Exp Zool 268 :486-491). We found that this activity can be preserved when sperm is frozen on dry ice with 0.6 M sucrose-10% dimethylsulfoxide (DMSO) extender (sperm :extender ratio 1 :3), and subsequently stored in liquid nitrogen. However, other methods of freezing (without cryoprotectant at -18°C, -80°C, and -196°C) did not protect this activity. Acrosin-like activity decreased in the course of storage of milt on ice ; 88% decline was recorded after 13 days. Acrosin-like activity increased with temperature from 10°C to 30°C, but was inactivated at 40°C to about 40% as compared to the optimum temperature. Triton X-100 inhibited activity by 15% and 72% at 0.01% and 0.1% concentrations, respectively. Activity was not affected by Mg<sup>2+</sup>
 but was inhibited by Zn<sup>2+</sup>
 (30% and 75% in the presence of 0.1 mM and 1 mM, respectively). Maximum velocity of substrate hydrolysis was observed at 2 mM of BAPNA. Acrosin-like activity was effectively inhibited by 4'-acetamidophenyl 4-guanidinobenzoate (AGB), an inhibitor of mammalian acrosin. Sperm acrosin-like activity correlated negatively with anti-proteinase activity of seminal plasma. We conclude that sturgeon acrosin-like activity shares many properties with mammalian acrosin. On the other hand, it has some unique properties which may represent adaptations of this enzyme to the environment of external fertilization.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002A29A</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Spermatozoïde</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Spermatozoa</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Espermatozoide</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Acrosin</s0>
<s2>FE</s2>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Acrosin</s0>
<s2>FE</s2>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Acrosin</s0>
<s2>FE</s2>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Trypsin</s0>
<s2>FE</s2>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Trypsin</s0>
<s2>FE</s2>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Trypsin</s0>
<s2>FE</s2>
<s5>03</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Homologie</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Homology</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Homología</s0>
<s5>04</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Activité enzymatique</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Enzymatic activity</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Actividad enzimática</s0>
<s5>05</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE"><s0>Régulation</s0>
<s5>07</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG"><s0>Regulation(control)</s0>
<s5>07</s5>
</fC03>
<fC03 i1="06" i2="X" l="GER"><s0>Regelung</s0>
<s5>07</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>Regulación</s0>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="FRE"><s0>Cryoconservation</s0>
<s5>08</s5>
</fC03>
<fC03 i1="07" i2="X" l="ENG"><s0>Cryopreservation</s0>
<s5>08</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA"><s0>Crioconservación</s0>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="X" l="FRE"><s0>Conservation sperme</s0>
<s5>17</s5>
</fC03>
<fC03 i1="08" i2="X" l="ENG"><s0>Sperm conservation</s0>
<s5>17</s5>
</fC03>
<fC03 i1="08" i2="X" l="SPA"><s0>Conservación esperma</s0>
<s5>17</s5>
</fC03>
<fC03 i1="09" i2="X" l="FRE"><s0>Pisces</s0>
<s2>NS</s2>
<s5>54</s5>
</fC03>
<fC03 i1="09" i2="X" l="ENG"><s0>Pisces</s0>
<s2>NS</s2>
<s5>54</s5>
</fC03>
<fC03 i1="09" i2="X" l="SPA"><s0>Pisces</s0>
<s2>NS</s2>
<s5>54</s5>
</fC03>
<fC03 i1="10" i2="X" l="FRE"><s0>Mâle</s0>
<s5>55</s5>
</fC03>
<fC03 i1="10" i2="X" l="ENG"><s0>Male</s0>
<s5>55</s5>
</fC03>
<fC03 i1="10" i2="X" l="SPA"><s0>Macho</s0>
<s5>55</s5>
</fC03>
<fC03 i1="11" i2="X" l="FRE"><s0>Acipenser fulvescens</s0>
<s2>NS</s2>
<s4>INC</s4>
<s5>81</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Serine endopeptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Serine endopeptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Serine endopeptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Proteinases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Proteinases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Proteinases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Enzyme</s0>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Enzyme</s0>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Enzima</s0>
</fC07>
<fC07 i1="05" i2="X" l="FRE"><s0>Cellule germinale</s0>
<s5>20</s5>
</fC07>
<fC07 i1="05" i2="X" l="ENG"><s0>Germinal cell</s0>
<s5>20</s5>
</fC07>
<fC07 i1="05" i2="X" l="SPA"><s0>Célula germinal</s0>
<s5>20</s5>
</fC07>
<fC07 i1="06" i2="X" l="FRE"><s0>Température</s0>
<s5>21</s5>
</fC07>
<fC07 i1="06" i2="X" l="ENG"><s0>Temperature</s0>
<s5>21</s5>
</fC07>
<fC07 i1="06" i2="X" l="GER"><s0>Temperatur</s0>
<s5>21</s5>
</fC07>
<fC07 i1="06" i2="X" l="SPA"><s0>Temperatura</s0>
<s5>21</s5>
</fC07>
<fC07 i1="07" i2="X" l="FRE"><s0>Facteur milieu</s0>
<s5>22</s5>
</fC07>
<fC07 i1="07" i2="X" l="ENG"><s0>Environmental factor</s0>
<s5>22</s5>
</fC07>
<fC07 i1="07" i2="X" l="SPA"><s0>Factor medio</s0>
<s5>22</s5>
</fC07>
<fC07 i1="08" i2="X" l="FRE"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="08" i2="X" l="ENG"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="08" i2="X" l="SPA"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fN21><s1>295</s1>
</fN21>
</pA>
</standard>
<server><NO>PASCAL 96-0429133 INIST</NO>
<ET>Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa</ET>
<AU>CIERESZKO (A.); DABROWSKI (K.); OCHKUR (S. I.)</AU>
<AF>School of Natural Resources, Ohio State University/Columbus, Ohio/Etats-Unis (1 aut., 2 aut.); Center of Agrotechnology and Veterinary Sciences, Polish Academy of Sciences/Olsztyn/Pologne (1 aut.); Institut for Problems of Cryobiology and Cryomedicine, Ukrainian Academy of Sciences/Kharkov/Ukraine (3 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Molecular reproduction and development; ISSN 1040-452X; Etats-Unis; Da. 1996; Vol. 45; No. 1; Pp. 72-77; Bibl. 34 ref.</SO>
<LA>Anglais</LA>
<EA>Acipenserid fish sperm possess trypsin-like activity, resembling acrosin activity of mammalian sperm, which can be measured by hydrolysis of N-α-benzoyl-DL-arginine p-nitroanilide (BAPNA) (Ciereszko et al., 1994 : J Exp Zool 268 :486-491). We found that this activity can be preserved when sperm is frozen on dry ice with 0.6 M sucrose-10% dimethylsulfoxide (DMSO) extender (sperm :extender ratio 1 :3), and subsequently stored in liquid nitrogen. However, other methods of freezing (without cryoprotectant at -18°C, -80°C, and -196°C) did not protect this activity. Acrosin-like activity decreased in the course of storage of milt on ice ; 88% decline was recorded after 13 days. Acrosin-like activity increased with temperature from 10°C to 30°C, but was inactivated at 40°C to about 40% as compared to the optimum temperature. Triton X-100 inhibited activity by 15% and 72% at 0.01% and 0.1% concentrations, respectively. Activity was not affected by Mg<sup>2+</sup>
 but was inhibited by Zn<sup>2+</sup>
 (30% and 75% in the presence of 0.1 mM and 1 mM, respectively). Maximum velocity of substrate hydrolysis was observed at 2 mM of BAPNA. Acrosin-like activity was effectively inhibited by 4'-acetamidophenyl 4-guanidinobenzoate (AGB), an inhibitor of mammalian acrosin. Sperm acrosin-like activity correlated negatively with anti-proteinase activity of seminal plasma. We conclude that sturgeon acrosin-like activity shares many properties with mammalian acrosin. On the other hand, it has some unique properties which may represent adaptations of this enzyme to the environment of external fertilization.</EA>
<CC>002A29A</CC>
<FD>Spermatozoïde; Acrosin; Trypsin; Homologie; Activité enzymatique; Régulation; Cryoconservation; Conservation sperme; Pisces; Mâle; Acipenser fulvescens</FD>
<FG>Serine endopeptidases; Proteinases; Hydrolases; Enzyme; Cellule germinale; Température; Facteur milieu; Vertebrata</FG>
<ED>Spermatozoa; Acrosin; Trypsin; Homology; Enzymatic activity; Regulation(control); Cryopreservation; Sperm conservation; Pisces; Male</ED>
<EG>Serine endopeptidases; Proteinases; Hydrolases; Enzyme; Germinal cell; Temperature; Environmental factor; Vertebrata</EG>
<GD>Regelung</GD>
<SD>Espermatozoide; Acrosin; Trypsin; Homología; Actividad enzimática; Regulación; Crioconservación; Conservación esperma; Pisces; Macho</SD>
<LO>INIST-18057.354000065788360100</LO>
<ID>96-0429133</ID>
</server>
</inist>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Wicri/Eau/explor/EsturgeonV1/Data/PascalFrancis/Corpus

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000488 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/PascalFrancis/Corpus/biblio.hfd -nk 000488 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Wicri/Eau
   |area=    EsturgeonV1
   |flux=    PascalFrancis
   |étape=   Corpus
   |type=    RBID
   |clé=     Pascal:96-0429133
   |texte=   Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa
}}

This area was generated with Dilib version V0.6.27.
Data generation: Sat Mar 25 15:37:54 2017. Site generation: Tue Feb 13 14:18:49 2024

	Serveur d'exploration sur l'esturgeon
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur l'esturgeon

Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa

Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa

Source :

Descripteurs français

English descriptors

Abstract

Notice en format standard (ISO 2709)

Format Inist (serveur)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri