1887

Abstract

Properties of the penicillin-binding proteins (PBPs) were studied. Several strains possessed at least five major PBPs, as shown previously for CB15, namely PBP1A, PBP1Bs, PBP2, PBP3 and PBP4. PBP4 was not detected in the strain CB13. None of the strains examined possessed the major PBPs of low molecular weight which have been found in other species of bacteria. The biochemical properties of the PBPs were studied further with two strains, CB13 and CB15. In these strains, PBPs of similar molecular weight were similar in properties such as affinity for β-lactam antibiotics and heat sensitivity. These properties were markedly different from those of PBPs of and other bacteria. To elucidate the functions of the PBPs, the effects of several β-lactam antibiotics on cell morphology and their affinities for different PBPs were examined. The relationship between the antibiotic effect and its affinity for PBPs suggests that PBP3 is involved in the process of cell division.

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/content/journal/micro/10.1099/00221287-126-1-111
1981-09-01
2019-10-18
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