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Biomedical subjects

R Moreno

Publications and source records attributed to R Moreno.

At least 199 records · Page 11Linked to original sources
PubMed1983

Neuropsychological study in patients with ALL. Two different CNS prevention therapies--cranial irradiation plus IT methotrexate vs. IT methotrexate alone.

Neurological, psychopedagogic, and psychologic long-term sequelae were evaluated in two groups of ALL patients in continuous CR for more than 2 years treated with two different CNS prophylaxis schemes. Group A, 19 patients (protocol 10-LLA-72 GATLA) received cranial irradiation 2400 rads plus IT MTX-DMT, and group B, 23 patients (protocol 1-LLA-76-GATLA) IT MTX-DMT only during induction and maintenance. All the patients were evaluated by performing neurological examination, EEG, EMG with nerve conduction velocity, CT scans, CSF studies, psychometric and psychologic studies, and neuropsychological evaluation. The most important findings were: 11 patients from group A (58%) showed abnormal CT (low density areas in the periventricular white matter, widening of subarachnoid space, ventricular dilatation, intracerebral calcification) and only one patient from group B showed CT abnormalities (p less than 0.0005). The neuropsychologic evaluation (performed by L. Bender technique and Picq-Vayer scale) showed more severe impairment (grade 3-4) in eight patients from group A (42%) and none in group B (p less than 0.001). Higher incidence of abnormalities in group A suggests the existence of more severe sequelae in the patients treated with cranial irradiation plus IT MTX-DMT than with IT MTX-DMT alone.

Adolescent↗
PubMed1974

Molecular weight, amino acid composition and physicochemical properties of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39.

The exocellular dd-carboxypeptidase-transpeptidase from Streptomyces R39 was purified to protein homogeneity and in milligram amounts. The isolated enzyme consisted of one polypeptide chain of molecular weight about 53300. Its amino acid composition and several physicochemical properties were determined and compared with those of the exo-cellular dd-carboxypeptidase-transpeptidase from Streptomyces R61.

Amino Acids↗
PubMed1974

Binding of beta-lactam antibiotics to the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39.

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 antibiotic. Spectrophotometric studies showed that binding of cephaloridine and cephalosporin 87-312 to the enzyme caused opening of their beta-lactam rings. Benzylpenicillin and cephalosporin 87-312 competed for the same site on the free enzyme, suggesting that binding of benzylpenicillin also resulted in the opening of its beta-lactam ring. In Tris-NaCl-MgCl(2) buffer at pH7.7 and 37 degrees C, the rate constants for the dissociation of the antibiotic-enzyme complexes were 2.8x10(-6), 1.5x10(-6) and 0.63x10(-6)s(-1) (half-lives 70, 130 and 300h) for benzylpenicillin, cephalosporin 87-312 and cephaloridine respectively. During the process, the protein underwent reactivation. The enzyme that was regenerated from its complex with benzylpenicillin was as sensitive to fresh benzylpenicillin as the native enzyme. With [(14)C]benzylpenicillin, the released radioactive compound was neither benzylpenicillin nor benzylpenicilloic acid. The Streptomyces R39 enzyme thus behaved as a beta-lactam-antibiotic-destroying enzyme but did not function as a beta-lactamase. Incubation at 37 degrees C in 0.01m-phosphate buffer, pH7.0, and in the same buffer supplemented with sodium dodecyl sulphate caused a more rapid reversion of the [(14)C]benzylpenicillin-enzyme complex. The rate constants were 1.6x10(-5)s(-1) and 0.8x10(-4)s(-1) respectively. Under these conditions, however, there was no concomitant reactivation of the enzyme and the released radioactive compound(s) appeared not to be the same as before. The Streptomyces R39 enzyme and the exocellular dd-carboxypeptidase-transpeptidase from Streptomyces R61 appeared to differ from each other with regard to the topography of their penicillin-binding site.

Binding, Competitive↗
PubMed1973

DD-carboxypeptidase-transpeptidase and killing site of beta-lactam antibiotics in Streptomyces strains R39, R61, and K11.

Additional evidence is given that in Streptomyces strains R39, R61, and K11 the same enzyme performs dd-carboxypeptidase and transpeptidase activities and that this enzyme is the killing site of beta-lactam antibiotics. With strain R61, it was found that the exocellular enzyme has a sensitivity towards some antibiotics different from that of the membrane-bound enzyme. Under the growth conditions used in the present investigations, beta-lactamase activity was not involved in susceptibility to beta-lactam antibiotics.

Acyltransferases↗