Abstract
Fraction I protein isolated from spinach beet chloroplasts was purified by ammonium sulphate fractionation and Sephadex G�200 gel filtration. The isolated protein was reduced and S-carboxymethylated, and the dissociated protein resolved into two distinct subunits by gel filtration on Sephadex G-200 in an 8M urea buffer at pH 10�0.
Subject
Developmental Biology,Endocrinology,Genetics,General Materials Science,Molecular Biology,Animal Science and Zoology,Reproductive Medicine,General Medicine,Biotechnology
Cited by
49 articles.
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