Abstract
Lactenin is reversibly inactivated by the exclusion of atmospheric oxygen. It is also inactivated by the sulfur-containing reducing agents cysteine, glutathione, thioglycollic acid, and BAL. Group A streptococci which have been acted upon by lactenin have been killed, and not merely prevented from multiplying, since they cannot be revived by inactivating lactenin through the addition of a reducing agent. Thiamine in great excess inactivates lactenin. The mechanism by which it accomplishes this has not been discovered, but it suggests that the mode of action of lactenin may be to deny thiamine to the lactenin-sensitive cell. Lactenin sensitivity is not, however, related to a requirement for exogenous thiamine, nor does lactenin appear to function by binding environmental thiamine in a form unavailable to the sensitive cell.
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