Hepatic breast cancer dissemination after an iatrogenic hepatic laceration during talc pleurodesis: a case report

<p>Abstract</p> <p>Background</p> <p>Talc pleurodesis is an effective treatment for malignant pleural effusion. We present a case of an asymptomatic hepatic laceration that occurred during pleurodesis in a breast cancer patient and led to hepatic tumor dissemination.</p> <p>Discussion</p> <p>Pleurodesis is a relatively safe procedure, although previous studies have described malignant invasion of scar tissue.</p> <p>Conclusion</p> <p>To our knowledge, this is the first case report of tumor spread due to a liver puncture during talc pleurodesis in a breast cancer patient.</p

Model-based diagnosis of acute pulmonary embolism - results from a porcine model

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The wall peptidoglycans of Neisseria perflava, Moraxella glucidolytica, Pseudomonas alcaligenes and Proteus vulgaris strain P18

The primary structure of the wall peptidoglycans of Neisseria perflava, Moraxella glucidolytica and Pseudomonas alcaligenes is similar to those of the Enterobacteriaceae Proteus vulgaris and Escherichia coli, suggesting that the peptidoglycans of all gram-negative bacteria contain meso-diaminopimelic acid and belong to the same chemotype I. Differences are observed with regard to the thickness of the peptidoglycan layer in the cell envelopes, the extent of peptide crosslinking and the occurrence of N,O-diacetylmuramic acid residues

Secretion by Overexpression and Purification of the Water-Soluble Streptomyces K15 Dd-Transpeptidase/Penicillin-Binding Protein

Though synthesized with a cleavable signal peptide and devoid of membrane anchors, the 262-amino-acid-residue Streptomyces K15 DD-transpeptidase/penicillin-binding protein is membrane-bound. Overexpression in Streptomyces lividans resulted in the export of an appreciable amount of the synthesized protein (4 mg/litre of culture supernatant). The water-soluble enzyme was purified close to protein homogeneity with a yield of 75%. It requires the presence of 0.5 M-NaCl to remain soluble. It is indistinguishable from the detergent-extract wild-type enzyme with respect to molecular mass, thermostability, transpeptidase activity and penicillin-binding capacity

The penicillin receptor in Streptomyces

Kinetics and optical studies of Streptomyces DD-carboxypeptidases-transpeptidases led to the conclusion that the donor, acceptor, and penicillin sites on these enzymes are different but not independent and that penicillin acts as a modifier of the conformation of the protein. In the presence of penicillin, the penicillin-sensitive enzymes would be frozen in a conformation that prevents catalytic activity

The peptidoglycan crosslinking enzyme system in Streptomyces R61, K15 and rimosus. Immunological studies

The exocellular DD-carboxypeptidases from Streptomyces R61, K 15, the lysozyme-releasable DD-carboxypeptidases from Streptomyces R61, K15 and rimosus, and the membrane-bound DD-carboxypeptidase of Streptomyces K15 are immunologically related to each other

Virtual reality surgical simulation as a tuition aid for understanding surgical temporal bone anatomy: trial on 15 ear, nose, and throat registrars

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