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Phosphorylation of yeast protein: Reduction of ribonucleic acid and isolation of yeast protein concentrate
Author(s) -
Huang Y.T.,
Kinsella J. E.
Publication year - 1986
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260281112
Subject(s) - yeast , lysine , biochemistry , phosphorylation , nucleic acid , amino acid , nucleoprotein , chemistry , rna , biology , dna , gene
Yeast nucleoproteins were chemically phosphorylated with phosphorus oxychloride (POCL 3 ). Studies using 31 P nuclear magnetic resonance (NMR) spectroscopy, stability to pH and lysine estimation all indicated that the ϵ‐amino group of lysine was the principal functional group phosphorylated. Phosphorylation of ca. 30% of the lysine residues resulted in removal of more than 85% of contaminant ribonucleic acid from protein precipitated at pH 4.2. Phosphorylation did not alter the amino acid composition of yeast proteins and was reversible under acidic conditions. Based on the data, a method for the preparation of phosphorylated yeast protein with low levels of nucleic acid is proposed.