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Biomedical subjects

A Scala

Publications and source records attributed to A Scala.

At least 91 records · Page 5Linked to original sources

Diesters of glycosylglycerols active in cancer chemoprevention.

Enzymatic transesterification, mediated by Pseudomonas cepacia lipase (lipase PS), led to the pure 1,6'-diacylderivatives of 2-O-beta-D-glucosyl-sn-glycerol and 2-O-beta-D-galactosyl-sn-glycerol, the acyl chains being derived from short-medium length fatty acids. A study of the in vitro inhibitory effects of these diacylderivatives on Epstein-Barr virus early antigen activation induced by the tumour promoter 12-O-tetradecanoylphorbol-13-acetate revealed that maximum activity was reached for the hexanoyl chain and that the introduction of a second acyl chain did not significantly modify the inhibitory potential referring to the corresponding 1- or 6'-monoesters.

Antigens, Viral↗

[Respiratory allergies in the Flegrean region].

The Authors value 407 consecutive outpatients, with rhinitis, conjunctivitis and asthma, coming from Flegrean area. In the patients with prick test positivity for pollen or inhalants the results were compared with clinical symptomatology. The data obtained, confirm the importance of inhalants persistent in asthma, and the rilevance of seasonal pollens in rhinoconjunctivitis and episodic asthma. In this homogeneous population, never the olea positivity was demonstrated as a single, whereas ambrosia (ragweed) was founded.

Adolescent↗

Endopolygalacturonase, an extracellular pectic enzyme of Rhizoctonia fragariae.

A pectolytic enzyme from culture filtrates of Rhizoctonia fragariae was purified approx. 29-fold. The enzyme exhibited maximal depolymerizing activity on Na-polypectate rather than pectin at pH 5.0 and was inhibited at different extent by divalent cations Mg++, Mn++, Ca++. The analysis by paper chromatography of the products of enzyme hydrolysis suggested that the enzyme attacks the substrate by a random mechanism. The absorption spectrum of the chromogen formed by the hydrolysis products and thiobarbituric acid suggested that the enzyme is a hydrolytic enzyme. On the basis of these results the enzyme is classifiable as endo-polygalacturonase (poly alpha-1,4-galacturonide glycanohydrolase E.C. 3.2.1.15).

Calcium↗