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Purification of an Endogenous polynucleotide phosphorylase from Brevibacterium JM98A
Author(s) -
H H Yang,
Donald W. Thayer,
Shiqiong Yang
Publication year - 1979
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.38.1.159-161.1979
Subject(s) - brevibacterium , polynucleotide phosphorylase , ribonucleoside , biochemistry , polynucleotide , chemistry , biology , enzyme , rna , bacteria , purine nucleoside phosphorylase , microorganism , genetics , purine , gene
Polynucleotide phosphorylase was purified form Brevibacterium JM98A (ATCC 29895). Homopolynucleotides were arsenolysed in the order polyadenylate greater than polycytidylic acid greater than polyuridylic acid greater than polyguanylate. The products were ribonucleoside 5'-monophosphates.

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