The induction, purification and characterization of 17β-hydroxy-C19-steroid dehydrogenase of the female guinea pig kidney

1979 ◽  
Vol 10 (2) ◽  
pp. 187-193 ◽  
Author(s):  
C.C. Shen ◽  
Charles D. Kochakian
Keyword(s):  
Guinea Pig ◽  
Purification And Characterization ◽  
Pig Kidney ◽  
Steroid Dehydrogenase

scholarly journals Purification and Characterization of the Primary Acrosomal Autoantigen of Guinea Pig Epididymal Spermatozoa1

1988 ◽  
Vol 38 (2) ◽  
pp. 423-437 ◽  
Author(s):  
Daniel M. Hardy ◽  
Thomas T. F. Huang ◽  
William J. Driscoll ◽  
Kenneth S. K. Tung ◽  
Gaynor C. Wild
Keyword(s):  
Guinea Pig ◽  
Purification And Characterization

Purification and characterization of guinea pig serum aminoacylproline hydrolase (aminopeptidase P)

1992 ◽  
Vol 1119 (2) ◽  
pp. 140-147 ◽  
Author(s):  
James W. Ryan ◽  
Fernando Valido ◽  
Pierre Berryer ◽  
Alfred Y.K. Chung ◽  
James E. Ripka
Keyword(s):  
Guinea Pig ◽  
Purification And Characterization ◽  
Aminopeptidase P ◽  
Pig Serum

scholarly journals Purification and characterization of pig kidney aminopeptidase P. A glycosyl-phosphatidylinositol-anchored ectoenzyme

1990 ◽  
Vol 267 (2) ◽  
pp. 509-515 ◽  
Author(s):  
N M Hooper ◽  
J Hryszko ◽  
A J Turner
Keyword(s):  
Chelating Agents ◽  
Inhibitory Effect ◽  
Purification And Characterization ◽  
Glycosyl Phosphatidylinositol ◽  
Pig Kidney ◽  
Sds Page ◽  
Cyclic Phosphate ◽  
Aminopeptidase P ◽  
Mild Acid

Aminopeptidase P (EC 3.4.11.9) was solubilized from pig kidney membranes with bacterial phosphatidylinositol-specific phospholipase C (PI-PLC) and then purified by a combination of anion-exchange and hydrophobic-interaction chromatographies. Contaminating peptidase activities were removed by selective affinity chromatography. The purified enzyme was apparently homogeneous on SDS/PAGE with an Mr of 91,000. Enzymic deglycosylation revealed that aminopeptidase P is a glycoprotein, with up to 25% by weight of the protein being due to the presence of N-linked sugars. The phospholipase-solubilized aminopeptidase P was recognized by an antiserum to the cross-reacting determinant (CRD) characteristic of the glycosyl-phosphatidylinositol anchor. This recognition was abolished by mild acid treatment or deamination with HNO2, indicating that the CRD was due exclusively to the inositol 1,2-cyclic phosphate ring epitope generated by the action of PI-PLC. The activity of aminopeptidase P was inhibited by chelating agents and was stimulated by Mn2+ or Co2+ ions, confirming the metallo-enzyme nature of this peptidase. Selective inhibitors of other aminopeptidases (actinonin, amastatin, bestatin and puromycin) had little or no inhibitory effect.

Sign in / Sign up

Export Citation Format

Share Document