Identification and partial characterization of alpha-1,4-glucosidase activity in equine epididymal fluid.
Theriogenology
; 61(7-8): 1545-58, 2004 May.
Article
em En
| MEDLINE
| ID: mdl-15036984
The expression of alpha-1,4-glucosidase activity was fluorometrically and electrophoretically assessed in the epididymal fluid and seminal plasma of stallions. alpha-Glucosidase specific activity in the epididymis increased significantly from the proximal caput to the cauda. Stallion epididymal glucosidase maintained activity in a wide range of pH, with two distinct peaks (around pH 4.0 and 6.0, respectively). Enzyme activities at different pH, inhibition assays with sodium dodecyl sulfate (SDS) and maltotriose (MTT, selective inhibitors of alpha-glucosidases "acidic" and "neutral" isoforms, described in other tissues) and the electrophoretic analysis in native and native/SDS-PAGE conditions, indicated that stallion epididymal glucosidase was due to two catalytically active forms. These forms, analyzed by non-denaturing electrophoresis, exhibited different electrophoretic mobility and molecular weight. Samples from the proximal caput of the epididymis were rich in Form II or "neutral" form, whereas the "acid" or Form I seemed to be predominate in the cauda epididymal region. At physiological pH, Form II was predominant in the seminal plasma. The physiological role(s) of these forms is uncertain, but based on their ability to hydrolyze glucosidic linkage, they probably are involved in degradation/modifications of epididymal fluid and/or spermatozoa glycoconjugates, thereby participating in plasma membrane remodeling associated with sperm maturation.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Epididimo
/
Alfa-Glucosidases
/
Cavalos
Tipo de estudo:
Diagnostic_studies
Limite:
Animals
Idioma:
En
Revista:
Theriogenology
Ano de publicação:
2004
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Estados Unidos