PURIFICATION AND PHYSICAL PROPERTIES OF GROUP C STREPTOCOCCAL PHAGE-ASSOCIATED LYSIN
A purification procedure for the Group C phage-associated lysin is described utilizing tetrathionate to protect the enzyme's -SH group(s) from thiol-inactivating agents. A 652-fold purification has been accomplished yielding a solution in which the enzyme activity corresponds to essentially a...
Main Authors: | , , |
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Format: | Online |
Language: | English |
Published: |
The Rockefeller University Press
1971
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Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138921/ |