Literature DB >> 3300643

Cross-reaction of a plant protein kinase with antiserum raised against a sequence from bovine brain protein kinase C regulatory sub-unit.

D C Elliott, Y S Kokke.   

Abstract

The partly purified calcium-dependent, phospholipid-activated protein kinase from A. tricolor seedlings contains three major protein species (Mr = 84,500, 65,000 and 40,000) which cross-react with antiserum raised against the regulatory domain of bovine brain protein kinase C. Two of these species (Mr = 84,500 and 40,000) were phosphorylated when the preparation was incubated with [gamma-32P] ATP. It is suggested that the three cross-reacting proteins correspond to native enzyme, partly proteolysed enzyme and regulatory sub-unit respectively.

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Year:  1987        PMID: 3300643     DOI: 10.1016/0006-291x(87)91541-5

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


  4 in total

Review 1.  The plant phosphoinositide system.

Authors:  B K Drøbak
Journal:  Biochem J       Date:  1992-12-15       Impact factor: 3.857

2.  The phosphorylation site of Ca(2+)-dependent protein kinase from alfalfa.

Authors:  Z Olah; L Bogre; C Lehel; A Farago; J Seprodi; D Dudits
Journal:  Plant Mol Biol       Date:  1989-04       Impact factor: 4.076

3.  Transmembrane Signaling via Phosphatidylinositol 4,5-Bisphosphate Hydrolysis in Plants.

Authors:  K J Einspahr; G A Thompson
Journal:  Plant Physiol       Date:  1990-06       Impact factor: 8.340

4.  A probable crosstalk between Ca⁺², reactive oxygen species accumulation and scavenging mechanisms and modulation of protein kinase C activity during seed development in sunflower.

Authors:  Anita Thakur; Satish C Bhatla
Journal:  Plant Signal Behav       Date:  2014-02-12
  4 in total

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