RT Journal Article SR Electronic(1) A1 Chapman, M. J. A1 Holt, R. J. A1 Mattocks, A. R. A1 Stewart, G. T.YR 1964 T1 Differentiation of Amidase and β-Lactamase by Infrared Absorption JF Microbiology, VO 36 IS 2 SP 215 OP 223 DO https://doi.org/10.1099/00221287-36-2-215 PB Microbiology Society, SN 1465-2080, AB SUMMARY: The carbonyl-β-lactam absorption band of penicillins and cephalosporins at 1760 cm.−1 is detectable when the antibiotics are mixed with enzymes or bacterial protein. This band can therefore be used for differentiating the two inactivating enzymes β-lactamase and amidase. Examined thus, methicil- lin, cloxacillin, amino-cephalosporanic acid (7-ACA) and thienylacetamido- 7-AC A were stable to staphylococcal β-lactamase but less stable to coliform β-lactamase. Only quinacillin among a range of therapeutic derivatives tested resisted both types of β-lactamase. The other inactivating enzyme, amidase, can exist independently of β-lactamase in coliform organisms. When methicillin and cloxacillin were treated with amidase, they lost their stability to β-lactamase., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-36-2-215