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Catalase activity in equine semen
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Abstract
Objective
—To characterize the activity of catalase in
equine semen.
Animals
—15 stallions of known and unknown reproductive
history.
Procedure
—Seminal plasma was collected from raw
equine semen by centrifugation, and samples of seminal
plasma were frozen prior to assay for catalase
activity. Tissue samples (n = 3 stallions) from the bulbourethral
gland, prostate gland, vesicular gland, and
testis were homogenized, and cauda epididymal fluid
was collected for determination of catalase activity.
Catalase activity was determined as an enzyme kinetic
assay by the disappearance of H
2
O
2
as measured
by ultraviolet spectrophotometry.
Results
—Catalase activity in equine seminal plasma
was 989.3 ± 167.8 U/ml (mean ± SEM), and the specific
activity of catalase in equine seminal plasma was
98.7 ± 29.2 U/mg of protein. Specific activity of catalase
in tissue homogenates was significantly higher in
the prostate gland (954 ± 270 U/mg of protein) than in
the ampulla (59 ± 5 U/mg of protein), bulbourethral
gland (54 ± 11 U/mg of protein), vesicular gland (39 ±
3 U/mg of protein), cauda epididymal fluid (11 ± 3
U/mg protein), or testis (54 ± 6 U/mg of protein).
Conclusions and Clinical Relevance
—Equine seminal
plasma contains a high activity of catalase that is
derived primarily from prostatic secretions.
Procedures such as semen cryopreservation that
remove most seminal plasma from semen may
reduce the ability to scavenge H
2
O
2
and thereby
increase the susceptibility of spermatozoa to oxidative
stress. (
Am J Vet Res
2000;61:1026–1030)
American Veterinary Medical Association (AVMA)
Title: Catalase activity in equine semen
Description:
Abstract
Objective
—To characterize the activity of catalase in
equine semen.
Animals
—15 stallions of known and unknown reproductive
history.
Procedure
—Seminal plasma was collected from raw
equine semen by centrifugation, and samples of seminal
plasma were frozen prior to assay for catalase
activity.
Tissue samples (n = 3 stallions) from the bulbourethral
gland, prostate gland, vesicular gland, and
testis were homogenized, and cauda epididymal fluid
was collected for determination of catalase activity.
Catalase activity was determined as an enzyme kinetic
assay by the disappearance of H
2
O
2
as measured
by ultraviolet spectrophotometry.
Results
—Catalase activity in equine seminal plasma
was 989.
3 ± 167.
8 U/ml (mean ± SEM), and the specific
activity of catalase in equine seminal plasma was
98.
7 ± 29.
2 U/mg of protein.
Specific activity of catalase
in tissue homogenates was significantly higher in
the prostate gland (954 ± 270 U/mg of protein) than in
the ampulla (59 ± 5 U/mg of protein), bulbourethral
gland (54 ± 11 U/mg of protein), vesicular gland (39 ±
3 U/mg of protein), cauda epididymal fluid (11 ± 3
U/mg protein), or testis (54 ± 6 U/mg of protein).
Conclusions and Clinical Relevance
—Equine seminal
plasma contains a high activity of catalase that is
derived primarily from prostatic secretions.
Procedures such as semen cryopreservation that
remove most seminal plasma from semen may
reduce the ability to scavenge H
2
O
2
and thereby
increase the susceptibility of spermatozoa to oxidative
stress.
(
Am J Vet Res
2000;61:1026–1030).
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