Abstract:
:We have purified from human placenta a low molecular mass substance that inhibits cAMP-dependent protein kinase and activates protein kinase C. This protein kinase regulator was purified in three steps: (1) homogenizing placentas in chloroform/methanol and extracting the regulator into water; (2) eluting a strong anion exchange high performance liquid chromatography (HPLC) column with a quaternary gradient; and (3) eluting a reversed-phase HPLC column with a binary gradient. The regulator was found to be highly purified by HPLC, thin-layer chromatography (TLC) and laser desorption ionization mass spectrometry with a molecular mass of 703 Daltons by the latter procedure. The physical and biochemical properties of this protein kinase regulator suggest that it is a phospholipid but it did not co-elute by HPLC or by TLC with any of the known phospholipid activators of protein kinase C.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Talwar N,Pilz RB,Yu Z,Burlingame A,Boss GRdoi
10.1023/a:1006836826926subject
Has Abstractpub_date
1997-05-01 00:00:00pages
75-83issue
1-2eissn
0300-8177issn
1573-4919journal_volume
170pub_type
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