Beta-lactamase with high molecular weight: evidence for an interaction with neuraminic acid-containing structures.
The constitutive beta-lactamase activity from Escherichia coli strain J53 (R6K) was separated into two fractions by gel filtration. One fraction (F') had a well known molecular weight 21,000; the other (F) had a molecular weight greater than 70,000. The F beta-lactamase gave a fraction similar to F' after neuraminidase treatment followed by gel filtration, suggesting that beta-lactamase molecules may be associated with neuraminic acid-containing structures. Such complexes could be an explanation for the multiple bands given in isoelectrofocusing of crude enzymatic extracts.
D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D004926:Escherichia coli / Q000201:enzymology; D007525:Isoelectric Focusing; D008970:Molecular Weight; D009439:Neuraminidase; D012794:Sialic Acids / Q000032:analysis*; D001618:beta-Lactamases / Q000032:analysis*
D012794:Sialic Acids; D009439:Neuraminidase; D001618:beta-Lactamases