LotaV3, Main, Exploration, bibRecord, 000E64

Serine proteinase inhibitors of seminal plasma of teleost fish: distribution of activity, electrophoretic profiles and relation to proteinase inhibitors of blood

Identifieur interne : 000E64 ( Main/Exploration ); précédent : 000E63; suivant : 000E65

Serine proteinase inhibitors of seminal plasma of teleost fish: distribution of activity, electrophoretic profiles and relation to proteinase inhibitors of blood

Auteurs : A. Ciereszko [Pologne] ; B. Piros [Pologne] ; K. Dabrowski [États-Unis] ; D. Kucharczyk [Pologne] ; M. J. Łuczy Ski [Pologne] ; S. Dobosz [Pologne] ; J. Glogowski [Pologne]

Source :

Journal of Fish Biology [ 0022-1112 ] ; 1998-12.

RBID : ISTEX:5261C45A351037CF6A585F0B55D468D8A6D213D4

Descripteurs français

Pascal (Inist)
- Abramis brama, Activité enzymatique, Comparaison interspécifique, Coregonus lavaretus, Cours eau, Electrophorégramme, Esox lucius, Gadidae, Hucho hucho, Inhibiteur enzyme, Liquide séminal, Lota lota, Oncorhynchus mykiss, Pologne, Protéine, Salmo trutta, Salvelinus fontinalis, Sang, Serine endopeptidases, Sperme, Teneur.
Wicri :
- geographic : Pologne.

English descriptors

KwdEn :
- Abramis brama, Blood, Content, Coregonus lavaretus, Electrophoretic pattern, Enzymatic activity, Enzyme inhibitor, Esox lucius, Interspecific comparison, Lota lota, Oncorhynchus mykiss, Poland, Protein, Salmo trutta, Salvelinus fontinalis, Semen, Seminal plasma, Serine endopeptidases, Stream, proteinase inhibitors, semen, teleost fish.

Abstract

Anti‐proteinase activity has been found in seminal plasma of eight teleost fish species: brown trout, rainbow trout, brook trout, lake whitefish, bream, northern pike, Danube salmon and burbot. This activity correlated with seminal plasma protein and sperm concentrations. Using a mammalian (bovine) trypsin for detecting proteinase inhibitors it was found for the first time that there are species‐specific electrophoretic profiles of anti‐proteinase activity. One to three bands could be identified by this method. However, additional proteinase inhibitors could be identified by using fish (cod) trypsin. These inhibitors were detected in seminal plasma of salmonids and coregonids and have a slow migration rate. Fast‐migrating proteinase inhibitors were present in rainbow, brown and brook trout, northern pike, whitefish and burbot. These inhibitors could be detected in brook and brown trout by using either trypsins. However, they were detected only with bovine trypsin in rainbow trout, northern pike, whitefish and burbot. These results suggest that multiple forms of serine proteinase inhibitors exist in seminal plasma of teleost fish and they differ in their affinity toward serine proteinases. Seminal plasma serine proteinase inhibitors of rainbow trout migrated during electrophoresis similarly to blood plasma proteinase inhibitors, and suggests that the two inhibitors may be similar or the same. Anti‐proteinase specific activity was similar in blood and seminal plasma. Proteinase inhibitors of fish seminal plasma seem to be an important part of sperm physiology, possibly related to protection of spermatozoa. Staining for detection of serine proteinase inhibitors also allowed detection of presence of nonspecific esterase in seminal plasma of most species.

Url:

https://api.istex.fr/document/5261C45A351037CF6A585F0B55D468D8A6D213D4/fulltext/pdf

DOI: 10.1111/j.1095-8649.1998.tb00249.x

Affiliations:

Pologne, États-Unis
Ohio

Le document en format XML

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<front><div type="abstract" xml:lang="en">Anti‐proteinase activity has been found in seminal plasma of eight teleost fish species: brown trout, rainbow trout, brook trout, lake whitefish, bream, northern pike, Danube salmon and burbot. This activity correlated with seminal plasma protein and sperm concentrations. Using a mammalian (bovine) trypsin for detecting proteinase inhibitors it was found for the first time that there are species‐specific electrophoretic profiles of anti‐proteinase activity. One to three bands could be identified by this method. However, additional proteinase inhibitors could be identified by using fish (cod) trypsin. These inhibitors were detected in seminal plasma of salmonids and coregonids and have a slow migration rate. Fast‐migrating proteinase inhibitors were present in rainbow, brown and brook trout, northern pike, whitefish and burbot. These inhibitors could be detected in brook and brown trout by using either trypsins. However, they were detected only with bovine trypsin in rainbow trout, northern pike, whitefish and burbot. These results suggest that multiple forms of serine proteinase inhibitors exist in seminal plasma of teleost fish and they differ in their affinity toward serine proteinases. Seminal plasma serine proteinase inhibitors of rainbow trout migrated during electrophoresis similarly to blood plasma proteinase inhibitors, and suggests that the two inhibitors may be similar or the same. Anti‐proteinase specific activity was similar in blood and seminal plasma. Proteinase inhibitors of fish seminal plasma seem to be an important part of sperm physiology, possibly related to protection of spermatozoa. Staining for detection of serine proteinase inhibitors also allowed detection of presence of nonspecific esterase in seminal plasma of most species.</div>
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Serine proteinase inhibitors of seminal plasma of teleost fish: distribution of activity, electrophoretic profiles and relation to proteinase inhibitors of blood

Serine proteinase inhibitors of seminal plasma of teleost fish: distribution of activity, electrophoretic profiles and relation to proteinase inhibitors of blood

Source :

Descripteurs français

English descriptors

Abstract

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