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Large-scale isolation of fraction 1 leaf protein (18S) from lucerne (Medicago sativa L)

Published online by Cambridge University Press:  27 March 2009

W. T. Jones
Affiliation:
Biochemistry Department, Institute of Animal Physiology, Agricultural Research Council, Babraham, Cambridge, England
J. L. Mangan
Affiliation:
Biochemistry Department, Institute of Animal Physiology, Agricultural Research Council, Babraham, Cambridge, England

Summary

Fraction 1 protein (18S) can be isolated in large quantities (order 100 g) in a soluble state by heating lucerne juice, adjusted to pH 6·7 to 6·9, from a Pirie extractor to 63 °C for 10 min. Low speed oentrifugation (2500 g) removed coagulated chloroplast fragments and most of the heat-denatured Fraction 2 proteins. Fraction 1 (18S) protein (> 95% pure) was purified from low molecular weight materials (sugars, phenolics etc.) by ammonium sulphate fractionation and gel filtration on Sephadex G-75 gels.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1976

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