## Abstract Externally oriented components on the human sperm cell surface and components in human seminal plasma were labeled by enzymatic iodination with lactoperoxidase and [^125^I] NaI. SDSβ7.5% PAGE of labeled sperm surface resolved one minor and four major components with approximate molecula
Characterization of human sperm plasma membrane: Glycolipids and polypeptides
β Scribed by Mack, S. R. ;Zaneveld, L. J. D. ;Peterson, R. N. ;Hunt, W. ;Russell, L. D.
- Publisher
- John Wiley and Sons
- Year
- 1987
- Tongue
- English
- Weight
- 667 KB
- Volume
- 243
- Category
- Article
- ISSN
- 0022-104X
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β¦ Synopsis
The plasma membranes from ejaculated human spermatozoa were removed by nitrogen cavitation (600 PSI for 10 min) and isolated by centrifugation followed by a discontinuous sucrose density gradient centrifugation. Glycolipid analysis of the plasma membrane revealed a three-fold enrichment in gangliosides: GM3 and GD1a/GD1b and neutral glycolipids: globoside and sulfatide as compared to that of whole human sperm. Two dimensional electrophoresis of human sperm plasma membranes revealed about 75 polypeptides. Several of these polypeptides were similar in migration and in display of shape and color to that found in boar sperm plasma membranes.
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Ejaculated human spermatozoa were subjected to nitrogen cavitation (600 psi for ten min) to remove the plasma membrane (PM). Electron microscopic examination of the cavitated cells revealed that 33% of the PM was removed from the sperm which includes both the head and tail regions. The released memb
## Abstract Mammalian spermatozoa attain the ability to fertilize an oocyte as they negotiate the female reproductive tract. This acquisition of functional competence is preceded by an intricate cascade of biochemical and functional changes collectively known as βcapacitation.β Among the universal
We have studied the mechanisms involved in calcium (Ca2+) transport through the basal plasma membranes (BPM) of the syncytiotrophoblast cells from full-term human placenta. These purified membranes were enriched 25-fold in Na+/ K+-adenosine triphosphatase (ATPase), 37-fold in [3H]dihydroalprenoloI b