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Studies on the flagellar ATPase of bull spermatozoa: Extraction and characterization

✍ Scribed by Young, Leona G. ;Smithwick, Eleanor B.

Publisher
John Wiley and Sons
Year
1983
Tongue
English
Weight
628 KB
Volume
226
Category
Article
ISSN
0022-104X

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✦ Synopsis

Abstract

Adenosine triphosphatase (ATPase) activity of flagella isolated from ejaculated bull sperm was solubilized by 5 min exposure to 0.6 M KC1 at 4Β°C. ATPase activity in the flagellar extract was characterized with respect to enzyme, substrate, activator ion, salt, and hydrogen ion concentration. Flagellar extract required the presence of a divalent cation for activity: Mg^2 +^, Ca^2 +^, or Mn^2+^ could function as activator, but Zn^2+^ or Cd^2+^ could not. Magnesium‐activated ATPase was maximal in the presence of Mg^2+^ and ATP in equilimolar concentrations and at alkaline pH. Calcium activated ATPase was maximal over a wide range of Ca^2 +^:ATP ratios and at pH 8.0. The presence of increasing concentrations of Na^+^ and/or K^+^ ions in the assay medium (0.5–300 mM) had no effect on the ATPase activity of flagellar extract.

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