Biomedical subjects
Publications and source records attributed to S Minami.
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The results of the brace treatment (Milwaukee brace, Thoraco-Lumbo-Sacral-Orthosis, Boston-Milwaukee brace) were studied in 509 patients with idiopathic scoliosis, who were braces for an average of 3 years and 3 months ranging from 2 to 10 years. Of these patients, 60 were followed up for about 24 months after the brace was discontinued. The distribution of these patients according to curve pattern was as follows: 319 had thoracic curve; 78 had lumbar curve (combining lumbar and thoracolumbar curves together as one group); and 112 had double major curve. The findings are summarized and conclusions were drawn as follows. 1. The best correction was obtained within a year after the initiation of bracing, followed by a gradual loss of correction. 2. There was a significant difference between the final correction rate and the best correction rate in the brace. 3. In the patients with ages ranging from 11 to 14 years and with curves of 30 degrees or less at the beginning of brace treatment, the curves were maintained within 30 degrees at the final stage. 4. Those patients who cooperated well in wearing their braces had a smaller loss of correction at the final stage. 5. In 63 per cent of the cases who showed progression in the brace, iliac apophysis did not appear at the beginning of brace treatment. 6. Moiré topography was used for the analysis of cosmesis and it was shown to be a valuable method of three dimensional evaluation. 7. In 60 patients who were followed up for 24 months on average after the brace was discontinued, the curves had improved an average of 1.6 degrees at the time of their last check up.
The enzyme reactions from NNM-A to NNM-E and from NNM-E to NNM-B were established in a cell-free system containing an extract from the nanaomycin producer Streptomyces rosa var. notoensis. The enzyme which catalyses the former epoxide-forming reaction (NNM-A leads to NNM-E) required NADH (or NADPH) and O2 suggesting that it is the monooxygenase-type; thus, NNM-A monooxygenase (4a,10a-epoxidizing) is proposed as its name. The other enzyme which catalyses the reductive epoxide-opening reaction (NNM-E leads to NNM-B) requires NADH or NADPH and is tentatively named NNM-B synthetase. Such a reductive epoxide-opening reaction is a novel enzyme reaction.
Nanaomycin D reductase, catalyzing the conversion of nanaomycin D to nanaomycin A, which is the first step in the biosynthetic sequence (D leads to A leads to E leads to B) in Streptomyces rosa var. notoensis, was purified from the crude extract of the strain by ammonium sulfate fractionation and column chromatography on DEAE-cellulose, Sephadex G-100 and hydroxyapatite to give an electrophoretically homogeneous preparation. The enzyme was found to be a flavoprotein which contains FAD as a prosthetic group and has a molecular weight of 68,000 daltons. It catalyzed the reductive transformation of nanaomycin D to nanaomycin A in the presence of NADH under anaerobic conditions. The Km values were 250 microM for nanaomycin D and 62 microM for NADH. The enzyme was inhibited by 1 mM Cu2+ ion and by NADH at concentrations over 50 microM. The optimal pH was 5.0 and the optimal temperature was 37 degrees C. Several benzoisochromane-quinone antibiotics other than nanaomycin D, kalafungin (enantiomer of nanaomycin D), griseucin A and frenolicin B were converted to the corresponding reduced products by the enzyme. However, granaticin and 4 alpha, 10 alpha-epoxynanaomycin D were not converted.
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Cephalosporin beat-lactamase (cephalosporinase, CSase) was purified from a strain of Pseudomonas aeruginosa resistant to beta-lactam antibiotics. The purified enzyme preparation gave a single protein band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its molecular weight was about 34,000. The specific activity was 49.7 mumoles/minute/mg of protein of the purified enzyme for the hydrolysis of cephaloridine. The optimal pH and optimal temperature were about 8.0 and 40 degrees C, respectively. Its isoelectric point was 8.7. The enzyme activity was inhibited by iodine, some divalent ions, and some semisynthetic beta-lactam antibiotics, including cephamycin derivatives such as moxalactam and YM09330. Mouse antiserum obtained against the purified enzyme showed no cross-reaction with other types of beta-lactamase in neutralization test.
According to the blocking test for proximity of cell surface antigens, L1210 leukemia-associated antigen was not linked to molecules carrying H-2d antigen or murine leukemia virus-associated antigen, but there was a close association between HVJ-associated antigen and L1210 leukemia-associated antigen on the surface membrane of HVJ-pi-infected L1210 leukemia cells. Once L1210 leukemia cells were infected with HVJ-pi, their adsorptive power was found to be greater than that of uninfected cells by quantitative absorption analysis. These phenomena may lead to a better recognition by the host of L1210 leukemia-associated antigen, followed by generation of tumor immunity.
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Cefoperazone (T-1551, CFP) a new semisynthetic cephalosporin, has a broad spectrum of antibacterial activity. We investigated the affinity of CFP to penicillin-binding proteins (PBPs) and the inhibition of peptidoglycan synthesis by CFP. CFP had high affinities for Escherichia coli PBP-3, -1Bs, -2, and -1A, in descending order, and low affinities for PBP-4, -5, and -6. Similarly, CFP showed high affinity for Pseudomonas aeruginosa PBP-3, -1A, -1B, -2, and -4, in descending order. It is known that E. coli PBP-3 and P. aeruginosa PBP-3 participate in cell division. These results are in good agreement with the formation of filamentous cells of E. coli and P. aeruginosa treated with CFP. CFP had lower inhibitory activities on D-alanine carboxypeptidase IA and IB of E. coli than that of penicillin G, but its inhibitory activities on the cross-link formation in peptidoglycan synthesis were the same as those of penicillin G and higher than those of ampicillin.
Cephalosporin beta-lactamase (cephalosporinase) was purified from a strain of Escherichia coli resistant to beta-lactam antibiotics. The purified enzyme preparation gave a single protein band on polyacrylamide gel electrophoresis, and its molecular weight was 39,000 from sodium dodecyl sulfate-acrylamide gel electrophoresis. Its isoelectric point was 8.7. The specific activity was 31.7 mumol/min per mg of protein of the purified enzyme for the hydrolysis of cephaloridine. The optimal pH was about 8.0, and the optimal temperature was 36 degrees C. The enzyme activity was inhibited by iodine, some divalent metallic ions, semisynthetic penicillins, cefuroxime-type cephalosporins, and cephamycin derivatives. The enzymological properties of the purified preparation have been compared with those of beta-lactamases from other gram-negative bacteria.
The induction of beta-lactamase in Enterobacter cloacae GN5797 was studied by using 23 beta-lactam antiobiotics, including newly introduced drugs, as inducers. the beta-lactam antibiotics can be classified into three groups on the basis of their inducer activity. Among the tested cephalosporins, cephamycin derivatives such as cefoxitin, cefmetazole, and YM09330 had high inducer activity even at low drug concentrations. On the other hand, cefoperazone, cefsulodin, piperacillin, and apalcillin showed low inducer activity when compared with the other cephalosporins.