Spontaneous hemopneumothorax with aberrant vessels found to be the source of bleeding: report of two cases.

We report herein our experience of two cases of spontaneous hemopneumothorax in which the source of bleeding was found to be aberrant vessels. Both patients were successfully treated by early thoracotomy. Case 1 was a 23-year-old female in whom chest X-ray revealed an air-fluid line and a bulla with a narrow restiform shadow connecting the pleural cupola. Angiography clearly visualized aberrant vessels branching from the costocervical trunk, distributed in and around the bulla in the apex of the lung, being the possible source of bleeding. These aberrant vessels were confirmed at surgery and resected. Case 2 was a 56-year-old male who underwent thoracotomy for persistent bleeding. At surgery, a continuously bleeding vessel from the pleural cupola was seen and ligated. The remnant of the vessel was located in the apex of the lung, and resected with the bulla. Thus, the rare entity of a congenital aberrant vessel lying concealed as a possible source of bleeding should be borne in mind.

Structural study of cell wall phosphomannan of Candida albicans NIH B-792 (serotype B) strain, with special reference to 1H and 13C NMR analyses of acid-labile oligomannosyl residues.

Chemical structures of manno-oligosaccharides, from biose to heptaose, released from the phosphomannan of Candida albicans NIH B-792 strain (serotype B) by mild acid hydrolysis were investigated. The results of 1H NMR, 13C NMR, and fast atom bombardment mass spectrometry analyses confirmed that these manno-oligosaccharides belong to a homologous beta-1,2-linked series. Although chemical shifts of 1H NMR patterns of these oligosaccharides were considerably too complicated to be assigned, their 13C NMR patterns were sufficiently simple to be interpreted, exhibiting a regular increase of downfield shift of ppm values of the C-1 atom from each mannopyranose residue in proportion to their molecular weights. In order to determine the whole chemical structure of the parent phosphomannan, the acid-stable domain was subjected to acetolysis and then enzymolysis with the Arthrobacter GJM-1 alpha-mannosidase and the resultant manno-oligosaccharides were investigated for their chemical structures by 1H NMR spectroscopy. The results of a precipitin-inhibition test using the beta-1,2-linked manno-oligosaccharides, from biose to hexaose, in comparison with the corresponding isomers containing alpha-1,2 linkage with small amounts of alpha-1,3 linkage, indicated that the haptens possessing the former linkage exhibited much higher inhibitory effects than the corresponding isomers containing the latter linkages did. Based on the present findings, a chemical structure of the phosphomannan of this C. albicans strain was proposed.

[Chondrosarcoma of the ribs: report of two cases].

Chondrosarcoma of rib origin is relatively rare in Japan. Two patients with chondrosarcoma of rib origin were treated surgically. Case 1: A 79-year-old male, 4 years ago, he noticed a tumor in the left anteroinferior part of the chest. The histological examination of the specimen obtained by incisional biopsy showed osteochondroma in another hospital and he had been under observation. Since the tumor has recently increased in size, he was referred to our department. Radical resection of the chest wall was performed. As expected, the tumor was found to be a secondary chondrosarcoma by postoperative histological examination. Case 2: A 49-year-old female. In the follow up studies after radical nephrectomy, Tc-MDP scintigram revealed an accumulation in the left second rib. Under the diagnosis of rib metastasis, radical resection was performed. The histological examination showed chondrosarcoma of rib origin postoperatively. This lesion was a primary central type, and is considered to have been resected in the earliest stage of all cases we have found in the Japanese literature.

Immunochemical properties of mannan-protein complex isolated from viable cells of Saccharomyces cerevisiae 4484-24D-1 mutant strain by the action of zymolyase.

Viable cells of Saccharomyces cerevisiae 4484-24D-1 mutant strain were treated with an Arthrobacter sp. beta-1,3-glucanase, Zymolyase-60,000, in the presence of a serine protease inhibitor, phenylmethylsulfonyl fluoride. Fractionation of the solubilized materials with Cetavlon (cetyltrimethylammonium bromide) yielded a purified mannan-protein complex, which had a molecular weight of ca. 150,000, approximately three times higher than that of the mannan isolated from the same cells by the hot-water extraction method at 135 C. The amino acid composition of the mannan-protein complex was found to be very similar to that of the mannan-protein complexes of S. cerevisiae X2180-1A wild and S. cerevisiae X2180-1A-5 mutant strains, indicating the presence of large amounts of serine and threonine. It was unexpected that the antibody-precipitating activity of this complex against the homologous anti-whole cell serum was about twice as great as that of the mannan isolated by hot-water extraction. Treatment of this complex with 100 mM NaOH, hot water at 135 C, and pronase, respectively, gave degradation products having the same molecular weight and antibody-precipitating activity as those of the hot-water extracted mannan, allowing the assumption that the protein moiety participated in a large part of this activity.

Isolation of mannan-protein complexes from viable cells of Saccharomyces cerevisiae X2180-1A wild type and Saccharomyces cerevisiae X2180-1 A-5 mutant strains by the action of Zymolyase-60,000.

The viable whole cells of Saccharomyces cerevisiae X2180-1A wild type and its mannan mutant strain S. cerevisiae X2180-1A-5, were treated with an Arthrobacter sp. beta-1,3-glucanase in the presence of a serine protease inhibitor, phenyl-methylsulfonyl fluoride. Fractionation of the solubilized materials of each strain with Cetavlon (cetyltrimethylammonium bromide) yielded one mannan-protein complex. Molecular weights of these complexes were almost the same as that of the mannoprotein of the mutant strain prepared by Nakajima and Ballou, which had a molecular weight of 133,000 and were approximately three times larger than those of the mannans isolated from the same cells by hot-water extraction. Each mannan-protein complex contained up to 2% glucose residue, which was not removed by specific precipitation with anti-mannan sera or by affinity chromatography on a column of concanavalin A-Sepharose. Treatment of these complexes with alkaline NaBH4 produced peptide-free mannan containing small amounts of glucose nearly identical to those of the parent complexes. The above findings provide evidence that the glucose residues exist in a covalently linked form to the mannan moiety. Fractionation of the mannan-protein complex of the S. cerevisiae wild-type strain by DEAE-Sephadex chromatography yielded five subfractions of different phosphate content, indicating that these highly intact mannan-protein complexes were of heterogeneous material consisting of many molecular species of different phosphate content.