Dansylalanyllysylchloromethyl ketone as a fluorescent probe for localization of acrosin activity in boar and human spermatozoa.
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منابع مشابه
P-11: DHR123: A Suitable Fluorescent Mitochondrial Probe for Assessment of H2O2 in Human Spermatozoa
Background: The objective of present study was to assess potential of DHR123 (dihydrorhodamine 123) fluorescent probe for measurement of H2O2 produced by human spermatozoa and comparing the results with DCFH-DA (2', 7'-dichlorodihydrofluorescein diacetate). Materials and Methods: Fluorescent intensity and percentage R123 and DCF positive sperm measured by flow cytometry. The suitable ...
متن کاملRelationship between acrosin activity of human spermatozoa and oxidative stress.
AIM To study the association between seminal oxidative stress and human sperm acrosin activity. METHODS It is a prospective study consisting of 30 infertile men and 12 fertile normozoospermic volunteers. A full history, clinical examination and scrotal ultrasound were done to exclude other related factors such as smoking and varicocele. Presence of white blood cells (WBCs) in semen samples wa...
متن کاملImmunocytochemical localization of acrosin in the anterior segment of the acrosomes of ram , boar and bull spermatozoa
Acrosin, a trypsin-like proteinase found in spermatozoa, is believed to play an essential role in fertilization by aiding the spermatozoon to penetrate the zona pellucida surrounding the egg (Mc Rorie and Williams, 1974). The precise cellular location of this enzyme is of considerable interest since such knowledge would aid in elucidating its mode of action. Biochemical studies have indicated t...
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The interactions of a fluorescent membrane probe, 1-anilinonaphthalene-8-sulfonic acid (1,8-ANS), with boar spermatozoa were followed through the use of lipoprotein fraction of ostrich egg yolk (LPFo). Semen samples, extended in Kortowo 3 (K3) extender, were supplemented with 2% or 5% LPFo and stored for 3h at 16 degrees C. Additionally, cold shock-treated spermatozoa (1h at 4 degrees C) were s...
متن کاملCharacterization and localization of adenylyl cyclase in membrane vesicles and intact boar and human spermatozoa.
The enzymic properties of adenylyl cyclase in purified membrane vesicles from human and boar spermatozoa are described. Plasma membrane vesicles, which appear to be right-side-out, show a marked increase in activity in the presence of the detergent Triton X-100, manganous ion and alkaline pH. Electron-microscope cytochemical assays indicated the presence of adenylyl cyclase in boar and human sp...
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ژورنال
عنوان ژورنال: Journal of Histochemistry & Cytochemistry
سال: 1984
ISSN: 0022-1554,1551-5044
DOI: 10.1177/32.5.6371133