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Biomedical subjects

B Joris

Publications and source records attributed to B Joris.

94 records · Page 6Linked to original sources
PubMed1981

The penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39.

Heat denaturation and Pronase degradation of the complex previously formed between benzylpenicillin and the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39 yields a heptapeptide H-Leu-Pro-Ala-Ser-Asn-Gly-Val-OH, where the benzylpenicilloyl group is ester-linked to the serine residue. This linkage is very labile and its hydrolysis causes the release of benzylpenicilloate. In contrast, the native benzylpenicilloyl-enzyme complex is very stable (half-life 70 h at 37 degrees C) and its breakdown proceeds via fragmentation of the bound benzylpenicilloyl group [Fuad, Frère, Ghuysen, Duez & Iwatsubo (1976) Biochem. J. 155, 623-629].

Amino Acid Sequence↗
PubMed1979

Parvalbumins from the lungfish (Protopterus dolloi).

Five parvalbumins have been isolated from the white muscles of the lungfish. They can be divided into two sub families showing typical amino acid compositions, C-terminal amino acid residues, peptide maps and immuno-reactivity. The red muscles including the cardiac muscle also contain parvalbumins in amounts roughly inversely related to the concentration of myoglobin in the muscle. Parvalbumins have also been detected in the brain and kidney.

Amino Acids↗
PubMedDate not supplied

Diversity of the mechanisms of resistance to beta-lactam antibiotics.

The sensitivity of a bacterium to beta-lactam antibiotics depends upon the interplay between 3 independent factors: the sensitivity of the essential penicillin-binding enzyme(s), the quantity and properties of the beta-lactamase(s) and the diffusion barrier that the outer-membrane of Gram-negative bacteria can represent. Those three factors can be modified by mutations or by the horizontal transfer of genes or portions of genes.

Anti-Bacterial Agents↗