One hundred and four patients presenting with either massive or repeated hemoptysis were treated by embolization of the bronchial arteries with a resorbable material (Spongel). The procedure was performed via selective catheterization of the abnormal arteries. Forty-nine patients were treated during and 55 after hemoptysis. Of the 49 patients treated during hemoptysis, immediate arrest of bleeding was affected in 41 but 6 of these patients suffered relapse two to seven months after the procedure. There was no recurrence of bleeding in the remaining 35 patients.

No abstract

No abstract

A cluster containing five similarly oriented genes involved in the metabolism of galactose via the Leloir pathway in Lactococcus lactis subsp. cremoris MG1363 was cloned and characterized. The order of the genes is galPMKTE, and these genes encode a galactose permease (GalP), an aldose 1-epimerase (GalM), a galactokinase (GalK), a hexose-1-phosphate uridylyltransferase (GalT), and a UDP-glucose 4-epimerase (GalE), respectively. This genetic organization reflects the order of the metabolic conversions during galactose utilization via the Leloir pathway. The functionality of the galP, galK, galT, and galE genes was shown by complementation studies performed with both Escherichia coli and L. lactis mutants. The GalP permease is a new member of the galactoside-pentose-hexuronide family of transporters. The capacity of GalP to transport galactose was demonstrated by using galP disruption mutant strains of L. lactis MG1363. A galK deletion was constructed by replacement recombination, and the mutant strain was not able to ferment galactose. Disruption of the galE gene resulted in a deficiency in cell separation along with the appearance of a long-chain phenotype when cells were grown on glucose as the sole carbon source. Recovery of the wild-type phenotype for the galE mutant was obtained either by genetic complementation or by addition of galactose to the growth medium.Understanding the mechanisms involved in carbohydrate metabolism and its regulation in lactic acid bacteria (LAB) is a prerequisite for improving the industrial properties of these organisms by metabolic engineering (16,29). The primary function of LAB in industrial dairy fermentations is conversion of lactose to lactic acid. Utilization of this disaccharide can occur in LAB via several mechanisms (18,47,48). The glucose moiety resulting from lactose hydrolysis is metabolized via glycolysis, whereas the galactose moiety follows different pathways depending on the LAB. While some thermophilic strains of LAB are known to release the galactose moiety of lactose into the medium (16,30,37), other LAB metabolize this disaccharide via two possible pathways depending on the mode of transport of the sugar (18, 48). When lactose or galactose is transported via a phosphoenolpyruvate-dependent phosphotransferase system (PTS), the resulting galactose 6-phosphate is metabolized by the enzymes of the tagatose 6-phosphate pathway (3, 51). In the case of galactose or lactose entry via a permease (18, 48), the sugar is not phosphorylated, and the galactose is degraded via the Leloir pathway (24).The Leloir pathway is among the first metabolic pathways that were discovered and includes three enzymes, galactokinase (GalK; EC 2.7.1.6), hexose-1-phosphate uridylyltransferase (GalT; EC 2.7.7.12), and UDP-glucose 4-epimerase (GalE; EC 5.1.3.2), which are involved in the conversion of galactose to glucose 1-phosphate. Aldose 1-epimerase or mutarotase (GalM; EC 5.1.3.3) is an additional enzyme required for rapid lactose metabolism and was characterized more recently (7,35,40). ...