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J. Biochem, 1984, Vol. 96, No. 4 1117-1124
© 1984 Japanese Biochemical Society

research-article

Characterization of Nuclear Phosphoprotein Phosphatases from Goat Testis

Uma BHATTACHARYYA and Gopal C. MAJUMDER1

Indian Institute of Chemical Biology 4, Raja S.C. Mullick Road, Jadavpur, Calcutta 700 032, India

1To whom correspondence should be addressed.

Two nuclear phosphoprotein phosphatases (PPases I and II) that cause dephosphorylation of (32P)histone, have been partially purified from goat testis. The enzymic activity is associated with nucleoplasm and chromatin. PPase I is markedly stimulated (approx. 200–600%) by Mg2+ or Mn2+ (1 mM) whereas Ca2+ (1mM) caused slight stimulation (approx. 35%) of the enzyme. On the contrary, PPase II is only slightly activated (20–40%) by these metal ions (5 mM). Both the phospho protein phosphatase isoenzymes are maximally active at pH 6–7. PPases I and II are strongly inhibited (approx. 60–100%) by ZnCl2 (1 mM), P1 (5 mM) and thiol reagents. NaF (5 mM) inhibits (approx. 40%) specifically the activity of PPase I rather than PPase II. PPases are strongly inhibited by relatively high concentration of NaCl (0.4 M), isoenzyme II being more sensitive (approx. 80%) than isoenzyme dephosphorylation of protamine, casein, and testicular nuclear proteins. Enzymic characteristics of the testicular nuclear PPases are clearly different from those of the cytosolic enzyme previously characterized.


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