Abstract:
:The purpose of this study is to report the development of a non-radioactive fluorescent peptide assay for measuring protein kinase C activity (PKC). The assay is based on a glycogen synthase derived fluorescent peptide that is phosphorylated by PKC. Phosphorylation causes the peptide to migrate toward the anode while the non-phosphorylated peptide migrates toward the cathode during agarose gel electrophoresis. Quantitation of PKC activity can be accomplished by excision of the appropriate bands and measuring their relative fluorescence. Using this assay, PKC activity was measured in whole cell homogenates from cultured renal mesangial cells. The enzyme(s)-substrate system followed Michaelis-Menten kinetics under limited conditions and, therefore, Lineweaver-Burk plots were used to obtain Michaelis constant and maximum velocity values. An apparent KM value of 40 microM was obtained for the fluorescent peptide substrate with a control Vmax value of 300 pmol/min. Addition of phorbol 12-myristate 13-acetate increased Vmax to 380 pmol/min.
journal_name
Life Scijournal_title
Life sciencesauthors
Isbell JC,Christian ST,Mashburn NA,Bell PDdoi
10.1016/0024-3205(95)02149-dsubject
Has Abstractpub_date
1995-01-01 00:00:00pages
1701-7issue
18eissn
0024-3205issn
1879-0631pii
002432059502149Djournal_volume
57pub_type
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