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Peptidase activities in the semen from the ductus deferens and uterus of the neotropical rattlesnake Crotalus durissus terrificus
- Source :
- Journal of Comparative Physiology B. 179:635-642
- Publication Year :
- 2009
- Publisher :
- Springer Science and Business Media LLC, 2009.
-
Abstract
- To understand the role of peptidases in seminal physiology of Crotalus durissus terrificus, intra- and inter-seasonal activity levels of acid (APA), basic (APB), puromycin-sensitive (APN-PS) and puromycin-insensitive neutral (APN-PI), cystyl (CAP), dipeptidyl-IV (DPPIV), type-1 pyroglutamyl (PAP-I) and prolyl-imino (PIP) aminopeptidases as well as prolyl endopeptidase (POP) were evaluated in soluble (SF) and/or membrane-bound (MF) fractions of semen collected from the ductus deferens of the male reproductive tract and from the posterior portion of the uterus. Seminal APB, PIP and POP were detected in SF, while other peptidases were detected in SF and MF. Only the convoluted posterior uterus in winter and autumn had semen. Relative to other examined peptidases, in general, APN-PI, APN-PS and APB activities were predominant in the semen from the uterus and throughout the year in the semen from the ductus deferens, suggesting their great relevance in the seminal physiology of C. d. terrificus. The levels of peptidase activities in the ductus deferens semen varied seasonally and were different from those of semen in the uterus, suggesting that their modulatory actions on susceptible peptides are integrated to the male reproductive cycle events and spermatozoa viability of this snake.
- Subjects :
- Male
medicine.medical_specialty
Physiology
Uterus
Semen
Biology
Reproductive cycle
Aminopeptidases
Biochemistry
Crotalus durissus terrificus
Male Reproductive Tract
Vas Deferens
Endocrinology
Prolyl endopeptidase
Internal medicine
medicine
Animals
Ecology, Evolution, Behavior and Systematics
urogenital system
Crotalus
Serine Endopeptidases
Human physiology
medicine.anatomical_structure
Female
Animal Science and Zoology
Seasons
Prolyl Oligopeptidases
medicine.drug
Subjects
Details
- ISSN :
- 1432136X and 01741578
- Volume :
- 179
- Database :
- OpenAIRE
- Journal :
- Journal of Comparative Physiology B
- Accession number :
- edsair.doi.dedup.....c182918947aa1ea559e103a06c16ded9