Structures of N-linked oligosaccharides of microsomal glycoproteins from developing castor bean endosperms.

The structures of sugar chains of the glycoproteins from the microsomal fraction of developing castor bean endosperms have been analyzed. The structural analyses were done by a fluorescence method combined with component analysis, exoglycosidase digestions, partial acetolysis, Smith degradation, and 1H-NMR spectroscopy. The estimated structures fell into three categories; the first was oligomannose-type, the second xylomannose-type, the third complex-type.

The effect of combinations of cefotiam and other antibiotics on methicillin-resistant Staphylococcus aureus in vitro.

The in-vitro activities of cefmetazole, flomoxef, imipenem, vancomycin and enramycin alone and in combination with cefotiam against eighteen clinically isolated methicillin-resistant Staphylococcus aureus was investigated. Cefotiam, cefmetazole, flomoxef and imipenem inhibited the growth of clinical isolates at concentrations ranging from 100 to 1600, 6.25 to 400, 6.

Induction of beta-lactamase in Proteus vulgaris.

Various beta-lactam antibiotics, including monocyclic beta-lactams, induced the beta-lactamase of Proteus vulgaris; when clinical isolates were induced by benzylpenicillin, each strain produced a single beta-lactamase but the activity per milligram dry weight differed from strain to strain. The beta-lactamases of the P. vulgaris strains were heterogeneous with respect to their isoelectric points, but had almost the same specific activities, substrate specificities and Michaelis constants.

Interactions of formylamino- and methoxy-substituted beta-lactam antibiotics with beta-lactamases.

Cephem and nocardicin-type monocyclic beta-lactam antibiotics with a formylamino substituent were highly resistant to hydrolysis by both penicillinases and cephalosporinases. Among antibiotics with a methoxy substituent, an N-sulfonated monocyclic beta-lactam antibiotic, sulfazecin was resistant to beta-lactamases, but cephem antibiotics were sensitive to the cephalosporinase of Enterobacter cloacae. The resistance of the antibiotics to the beta-lactamases depended primarily on the presence of the substituent, but affinity for the beta-lactamases was affected not only by the substituent but also by the presence of other side chains.