Literature DB >> 1543483

Cytosolic phospholipase A2 from U937 cells: size of the functional enzyme by radiation inactivation.

N M Tremblay1, D Nicholson, M Potier, P K Weech.   

Abstract

We have studied the cytosolic phospholipase A2 (cPLA2) of human U937 cells by radiation inactivation in order to characterize the functional form of the native enzyme by a method that was independent of the discrepancies observed by SDS-PAGE and cDNA cloning. The Radiation Inactivation Size of cPLA2 was reproducible and gave a value of 76,800-80,100 daltons. We eluted the active enzyme from polyacrylamide-gradient gel electrophoresis at a molecular weight of 77,000, confirming the irradiation result. We conclude that cPLA2 is active as the monomeric enzyme and is composed of a single major functional domain that is sensitive to irradiation.

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Year:  1992        PMID: 1543483     DOI: 10.1016/0006-291x(92)91617-y

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Cytosolic phospholipase A2 from human monocytic cells: characterization of substrate specificity and Ca(2+)-dependent membrane association.

Authors:  W Rehfeldt; K Resch; M Goppelt-Struebe
Journal:  Biochem J       Date:  1993-07-01       Impact factor: 3.857

2.  Inactivation of secretory phospholipase A2 by ionizing radiation.

Authors:  L J Reynolds; E S Kempner; L L Hughes; E A Dennis
Journal:  Biophys J       Date:  1995-05       Impact factor: 4.033

  2 in total

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