Results 11 to 20 of about 2,376 (199)
Epitope of antiphospholipid antibodies retrieved from peptide microarray based on R39‐R43 of β2‐glycoprotein I [PDF]
Research and Practice in Thrombosis and Haemostasis, 2022 Background Antiphospholipid antibody (aPL) syndrome (APS) is an autoimmune disease characterized by the presence of antiphospholipid antibodies and thromboembolic or pregnancy complications.
Marc Moghbel +8 more
doaj +7 more sources
Penicillin-sensitive DD-carboxypeptidases from Streptomyces strains R39 and K11 [PDF]
Biochemistry, 1972 The two penicillin-sensitive DD-carboxypeptidases from Streptomyces R39 and K11 are anionic at pH 8. They specifically recognize a C-terminal L-R3-D-alanyl-D sequence with a long side chain at the R3 position. The two enzymes differ from each other with respect to: (1) the effects of ionic strength on activity, (2) the influence exerted on activity by ...
Mélina Leyh-Bouille +2 more
exaly +4 more sources
Purification and properties of the exocellular β-lactamase of a Actinomadura strain R39 [PDF]
BBA - Proteins and Proteomics, 1982 The exocellular beta-lactamase (penicillin amido-beta-lactamhydrolase, EC 3.5.2.6) of Actinomadura R39 consists of one single polypeptide chain of molecular weight about 15 200. It exhibits a highly asymmetrical shape, has a low isoelectric point (at pH 5.0) and contains about 9.3% (w/w) of a polydeoxyribonucleotide with which it forms a rather stable ...
Colette Duez +2 more
exaly +4 more sources
R39. Ps. Arnaldus de Vilanova [PDF]
, 2007 This chapter presents a detailed repertory which gives incipit and explicit as well as information on author, date, editions and a summary of the contents of the dialogues on Philosopher's stone, Natural treasure, Secret operations, Secrets of matter and Instructed stone written by Arnaldus De Villanova in the Middle Ages.
C Cardelle De Hartmann
exaly +7 more sources
Site-directed mutagenesis of the Actinomadura R39 DD-peptidase [PDF]
Biochemical Journal, 1997 The role of various residues in the conserved structural elements of the Actinomadura R39 penicillin-sensitive DD-peptidase has been studied by site-directed mutagenesis. Replacement of Ser-298 of the ‘SDN loop’ by Ala or Gly significantly decreased the kcat/Km value for the peptide substrate, but only by a factor of 15 and had little effect on the ...
Zhao, GuoHua +7 more
openaire +5 more sources
The J-shape of β2GPI reveals a cryptic discontinuous epitope across domains I and II [PDF]
Journal of Structural Biology: XBeta-2-Glycoprotein I is the main target for pathogenic antiphospholipid syndrome autoantibodies. It can adopt several conformations, including an O-shape and two more linear J- and S-shapes.
C.J. Lalaurie +5 more
doaj +2 more sources
Binding of β-lactam antibiotics to the exocellular
Biochemical Journal, 1974 Benzylpenicillin and cephaloridine reacted with the exocellular dd-carboxypeptidase–transpeptidase from Streptomyces R39 to form equimolar and inactive antibiotic–enzyme complexes. At saturation, the molar ratio of chromogenic cephalosporin 87-312 to enzyme was 1.3:1, but this discrepancy might be due to a lack of accuracy in the measurement of the ...
Jean-Marie Frère +4 more
openaire +4 more sources
Kinetics of Reactions of the Actinomadura R39
Biochemistry, 2010 The Actinomadura R39 DD-peptidase catalyzes the hydrolysis and aminolysis of a number of small peptides and depsipeptides. Details of its substrate specificity and the nature of its in vivo substrate are not, however, well understood. This paper describes the interactions of the R39 enzyme with two peptidoglycan-mimetic substrates 3-(D-cysteinyl ...
Adediran, S. A. +4 more
openaire +6 more sources
The penicillin-binding site in the exocellular
Biochemical Journal, 1981 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.
Duez, Colette +4 more
openaire +5 more sources
Exocellular β-Lactamases of Streptomyces albus G and Strains R39 and K11 [PDF]
Antimicrobial Agents and Chemotherapy, 1973 The β-lactamases excreted by the highly benzylpenicillin-susceptible Streptomyces strain R39 and the highly benzylpenicillin-resistant Streptomyces albus G were isolated and purified. Neither β-lactamase exhibited dd -carboxypeptidase activity. Both were anionic at
Johnson, Kenneth +3 more
openaire +5 more sources