Specific staining of myo-inositol-1-phosphatase on polyacrylamide gels after electrophoresis |
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Authors: | L Parthasarathy T G Ramesh C S Shyamala Devi R Parthasarathy |
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Institution: | (1) Department of Biochemistry, University of Madras, Guindy Campus, 600 025 Madras, India;(2) Centre for Biotechnology, Anna University, 600 025 Madras, India |
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Abstract: | A sensitive staining method was developed to localise the activity of myo-inositol-1-phosphatase on Polyacrylamide gels after
electrophoresis. The method can also be used for non-specific phosphatases as well as for those specific phosphatases acting
upon inositol polyphosphates which are prime cellular second messengers. One or two nmol of phosphate is sufficient and less
than 3 μg of purified protein will facilitate the localisation of phosphatase. If more phosphatases are present in the enzyme
preparation, a combination of inhibitors can be used to suppress the activities of unwanted phosphatases and the use of specific
substrates will facilitate the localisation of enzyme of interest.
For nomenclature of myo-inositol phosphates recent recommendations are followed. ReferBiochem. J.,258, 1–2 (1989) andEur. J. Biochem.,180, 485–486 (1989). L-myo-inositol-1-phosphate is presently otherwise called as D-myo-inositol-3-phosphate. |
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Keywords: | Myo-inositol-1-phosphatase alkaline phosphatase rat testis levamisole lithium ions |
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