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Characterization of the ATP‐phosphohydrolase activity of bovine spermatozoa flagellar extracts
Author(s) -
Young Leona G.,
Smithwick Eleanor B.
Publication year - 1975
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1040850115
Subject(s) - flagellum , chemistry , biochemistry , adenosine triphosphate , microbiology and biotechnology , biology , gene
The ATP‐phosphohydrolase activity of extracts prepared from bovine spermatozoa flagella (BSFE), was characterized with respect to enzyme, substrate, activator ion and salt concentration, temperature dependence and time stability. BSFE required the presence of a divalent cation for activity: Mg ++ or Ca ++ could function as activator; Mn ++ , Zn ++ and Cd ++ could not. EDTA, but not EGTA, was inhibitory to enzymatic activity. Ca ++ inhibited the Mg ++ stimulated activity. ATP was dephosphorylated more rapidly than GTP>CTP>ITP, and ADP was dephosphorylated at 40% of the rate of ATP. The magnesium activated ATPase was stimulated by potassium and inhibited by sodium ions. Activation of BSFE ATP‐phosphohydrolase was maximal in the presence of Mg ++ and ATP in equimolar concentrations and K + (0.05–0.3 m) at 30°C. Although the enzymatic activity of the extract was found to decrease rapidly with time, it could be maintained for up to three days by the addition of 2‐β‐mercaptoethanol to the bovine spermatozoa flagellar extracts.