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Nucleic Acids Research, 1975, Vol. 2, No. 2 149-164
© 1975

Articles

Further characterization of the polynucleotide phosphorylase of Micrococcus luteus

Carol H. Letendrea and Maxine F. Singerb

National Institute of Arthritis, Metabolism, and Digestive Diseases, National Institutes of Health Bethesda, Maryland 20014, USA

Received December 10, 1974.

The purification of polynucleotide phosphorylase from Micrococcus luteus by chromatography on phosphocellulose columns is described. This procedure offers several advantages over previous procedures.

Previously determined molecular weights for Form-I enzyme and Form-T enzyme derived from Form-I by limited tryptic hydrolysis were confirmed as 2.7 and 2.3 x 105, respectively. Form-I appears homogeneous in the ultracentrifuge, but multiple active protein species are separable by polyacrylamide gel electrophoresis. The multiple species are probably the result of proteolysis. On polyacrylamide gel electrophoresis under denaturing conditions, Form-T yielded a single size of subunit of 71,000 daltons, and Form-I yielded several bands of different molecular sizes. These results differ from earlier determinations.

The amino acid compositions of Form-I and Form-T are reported. Form-I contains only between 8 and 10 cysteine residues per molecule and Form-T half that many.

aPresent address: National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20014.

bPresent address: National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20014.


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