Abstract
Protein phosphatase activity associated with neurofilament (NF) rich (Triton X-100 insoluble) fraction was extracted and partially characterised by using known inhibitors of protein phosphatases such as vanadate and fluoride. Protein phosphatase activity was demonstrated with reference to the dephosphorylation of endogenous substrate, NF protein and exogenous protein substrates, casein and phosvitin. Phosphoamino acids and beta-glycerophosphate were found to be poor substrates. Further, new observations have been made regarding the in vitro inhibitory effect of aluminium and the differential effects of some of the neuropsychoactive drugs. The findings could possibly lead to studies explaining the biochemical basis of aluminium induced neurotoxicity as well as the side effects associated with the long term medication of neuropsychoactive drugs.
MeSH terms
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Acetaldehyde / pharmacology
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Aldehydes / pharmacology
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Aluminum / pharmacology*
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Aluminum Chloride
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Aluminum Compounds*
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Animals
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Ascorbic Acid / pharmacology
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Cations / pharmacology*
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Cattle
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Chlorides / pharmacology*
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Ditiocarb / pharmacology
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Fluorides / pharmacology
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Glutathione / pharmacology
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Nerve Tissue Proteins / isolation & purification
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Nerve Tissue Proteins / metabolism*
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Neurofilament Proteins / isolation & purification
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Neurofilament Proteins / metabolism*
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Phosphoprotein Phosphatases / antagonists & inhibitors
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Phosphoprotein Phosphatases / isolation & purification
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Phosphoprotein Phosphatases / metabolism*
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Phosphoproteins / isolation & purification
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Phosphoproteins / metabolism*
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Phosphorylation
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Psychotropic Drugs / pharmacology*
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Spinal Cord / chemistry*
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Substrate Specificity
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Vanadates / pharmacology
Substances
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Aldehydes
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Aluminum Compounds
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Cations
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Chlorides
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Nerve Tissue Proteins
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Neurofilament Proteins
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Phosphoproteins
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Psychotropic Drugs
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Aluminum Chloride
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Vanadates
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Ditiocarb
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propionaldehyde
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Aluminum
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Phosphoprotein Phosphatases
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Glutathione
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Acetaldehyde
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Ascorbic Acid
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Fluorides