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Biomedical subjects

F Bermejo

Publications and source records attributed to F Bermejo.

At least 109 records · Page 6Linked to original sources
PubMed1989

[Myoclonic encephalopathy caused by bismuth salts. Efficacy of treatment with dimercaprol].

Three patients with myoclonic encephalopathy caused by bismuth salts are reported, one with the severe and another with the mild form; dimercaprol was effective for the rapid improvement of the symptoms in both. In one of the patients in whom the clearance of bismuth was calculated it was found to be increased after dimercaprol therapy. We think that dimercaprol is an effective drug for the therapy of myoclonic encephalopathy caused by bismuth salts.

Adult↗
PubMed1989

[Ictus].

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Cerebrovascular Disorders↗
PubMed1988

Enzymatic synthesis of penicillins.

Different penicillins (phenylacetyl, 2-hydroxyphenylacetyl, 4-hydroxyphenylacetyl, phenoxyacetyl and 2-thiopheneacetylpenicillin) have been synthesized "in vitro" by direct N-acylation of 6-aminopenicillanic acid (6-APA) with the acyl group of several acyl-CoA derivatives. The enzyme that catalyzes these reactions, acyl-CoA: 6-APA acyltransferase of Penicillium chrysogenum, was purified to homogeneity (374-fold) and its amino acid composition is given. This protein accepts as substrates several aliphatic acids and different aromatic acids with the only requirement that an acetyl-CoA moiety must be present in the substrate molecule. Shortening or lengthening of the acyl moiety prevents the 6-APA-N-acylation reaction. The presence of an amino group in the alpha-position of the acetyl group does not allow this molecule to be used as substrate. However, different substitutions in the phenyl group (hydroxylation of the carbons 2 and 4) or its replacement by another aromatic ring (thiophene) were accepted with varying reactions rates in the acylation reaction when a 176-fold purified acyltransferase was employed. The homogeneity pure enzyme accepts as substrate thiophene acetyl-CoA but it did not 2-hydroxyphenyl and 4-hydroxyphenylacetyl-CoA. The presence of an oxygen atom between the aromatic and the acetyl moieties did not affect the catalysis.

Acyltransferases↗